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Human Metabolome Database Version 2.5

 

Showing metabocard for Tetradecanoyl-CoA (HMDB01521)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:53
Accession Number HMDB01521
Secondary Accession Numbers HMDB06517
Common Name Tetradecanoyl-CoA
Description Tetradecanoyl-CoA (or myristoyl-CoA) is an intermediate in fatty acid biosynthesis, fatty acid elongation and the beta oxidation of fatty acids. It is also used in the myristoylation of proteins. The first pass through the beta-oxidation process starts with the saturated fatty acid palmitoyl-CoA and produces myristoyl-CoA. A total of four enzymatic steps are required, starting with VLCAD CoA dehydrogenase (Very Long Chain) activity, followed by three enzymatic steps catalyzed by enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and ketoacyl-CoA thiolase, all present in the mitochondria. Myristoylation of proteins is also catalyzed by the presence of myristoyl-CoA along with Myristoyl-CoA:protein N-myristoyltransferase (NMT). Myristoylation is an irreversible, co-translational (during translation) protein modification found in animals, plants, fungi and viruses. In this protein modification a myristoyl group (derived from myristioyl CoA) is covalently attached via an amide bond to the alpha-amino group of an N-terminal amino acid of a nascent polypeptide. It is more common on glycine residues but also occurs on other amino acids. Myristoylation also occurs post-translationally, for example when previously internal glycine residues become exposed by caspase cleavage during apoptosis. Myristoylation plays a vital role in membrane targeting and signal transduction in plant responses to environmental stress. Compared to other species that possess a single functional myristoyl-CoA: protein N-myristoyltransferase (NMT) gene copy, human, mouse and cow possess 2 NMT genes, and more than 2 protein isoforms.
Synonyms
  1. Myristoyl-CoA
  2. Myristoyl-coenzyme A
  3. S-Tetradecanoyl-coenzyme A
  4. n-C14:0CoA
  5. Tetradecanoyl CoA
  6. Tetradecanoyl-coenzyme A
  7. n-C14:0Coenzyme A
  8. Tetradecanoyl Coenzyme A
Chemical IUPAC Name [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-2-[[hydroxy-[hydroxy-[3-hydroxy-2,2-dimethyl-3-[2-(2-tetradecanoylsulfanylethylcarbamoyl)ethylcarbamoyl]propoxy]phosphoryl]oxy-phosphoryl]oxymethyl]oxolan-3-yl]oxyphosphonic acid
Chemical Formula C35H62N7O17P3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Coenzyme A Derivatives
Sub Class
  • Medium chain acyl CoAs
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • secondary carboxylic acid amide
  • thiocarboxylic acid ester
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Lipid biosynthesis, Fatty acid transport
Application
Source
  • Endogenous
Average Molecular Weight 977.890
Monoisotopic Molecular Weight 977.313599
Isomeric SMILES CCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N
Canonical SMILES CCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N
KEGG Compound ID C02593 Link Image
BioCyc ID TETRADECANOYL-COA Link Image
BiGG ID 40154 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01521 Link Image
Metagene Link HMDB01521 Link Image
METLIN ID 3707 Link Image
PubChem Compound 1126 Link Image
PubChem Substance 6450468 Link Image
ChEBI ID 15532 Link Image
CAS Registry Number 3130-72-1
InChI Identifier InChI=1/C35H62N7O17P3S/c1-4-5-6-7-8-9-10-11-12-13-14-15-26(44)63-19-18-37-25(43)16-17-38-33(47)30(46)35(2,3)21-56-62(53,54)59-61(51,52)55-20-24-29(58-60(48,49)50)28(45)34(57-24)42-23-41-27-31(36)39-22-40-32(27)42/h22-24,28-30,34,45-46H,4-21H2,1-3H3,(H,37,43)(H,38,47)(H,51,52)(H,53,54)(H2,36,39,40)(H2,48,49,50)/t24-,28-,29-,30?,34-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.21 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.84 [Predicted by ALOGPS]; -0.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID 1IIC Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Beta Oxidation of Very Long Chain Fatty Acids SMP00052 Link Image map01040 Link Image
Fatty Acid Elongation In Mitochondria SMP00054 Link Image map00062 Link Image
Fatty acid Metabolism SMP00051 Link Image map00071 Link Image
Mitochondrial Beta-Oxidation of Long Chain Saturated Fatty Acids SMP00482 Link Image
General References
  1. Hunt MC, Ruiter J, Mooyer P, van Roermond CW, Ofman R, Ijlst L, Wanders RJ: Identification of fatty acid oxidation disorder patients with lowered acyl-CoA thioesterase activity in human skin fibroblasts. Eur J Clin Invest. 2005 Jan;35(1):38-46. [PubMed Link Image]
Metabolic Enzymes
  1. 3-ketoacyl-CoA thiolase, mitochondrial
  2. Trifunctional enzyme subunit beta, mitochondrial
  3. Long-chain specific acyl-CoA dehydrogenase, mitochondrial
  4. Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
  5. Peroxisomal acyl-coenzyme A oxidase 1
  6. Peroxisomal acyl-coenzyme A oxidase 3
  7. Peroxisomal trans-2-enoyl-CoA reductase
  8. Glycylpeptide N-tetradecanoyltransferase 1
  9. Glycylpeptide N-tetradecanoyltransferase 2
  10. Acyl-Coenzyme A dehydrogenase, long chain
  11. ACAA1 protein
  12. cDNA FLJ76905, highly similar to Homo sapiens N-myristoyltransferase 1 (NMT1), mRNA (N-myristoyltransferase 1, isoform CRA_b)
  13. cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)
  14. Glycylpeptide N-tetradecanoyltransferase
  15. Glycylpeptide N-tetradecanoyltransferase
  16. Glycylpeptide N-tetradecanoyltransferase
  17. Glycylpeptide N-tetradecanoyltransferase
  18. Glycylpeptide N-tetradecanoyltransferase
  19. Glycylpeptide N-tetradecanoyltransferase
  20. Glycylpeptide N-tetradecanoyltransferase
Enzyme 1 [top]
Enzyme 1 ID 5260
Enzyme 1 Name 3-ketoacyl-CoA thiolase, mitochondrial
Enzyme 1 Synonyms
  1. Acetyl-CoA acyltransferase
  2. Beta-ketothiolase
  3. Mitochondrial 3-oxoacyl-CoA thiolase
  4. T1
Enzyme 1 Gene Name ACAA2
Enzyme 1 Protein Sequence >3-ketoacyl-CoA thiolase, mitochondrial
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
Enzyme 1 Number of Residues 397
Enzyme 1 Molecular Weight 41923.8
Enzyme 1 Theoretical pI 8.21
Enzyme 1 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 1 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 1 Specific Function Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 1 Pathways
  • Benzoate Degradation via Hydroxylation (map00362 Link Image)
  • Bile Acid Biosynthesis (map00120 Link Image)
  • Fatty Acid Elongation In Mitochondria (map00062 Link Image)
  • Fatty Acid Metabolism (map00071 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 12804931 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P42765 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name THIM_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1194 bp
ATGGCTCTGCTCCGAGGTGTGTTTGTAGTTGCTGCTAAGCGAACGCCCTTTGGAGCTTAC
GGAGGCCTTCTGAAAGACTTCACTGCTACTGACTTGTCTGAATTTGCTGCCAAGGCTGCC
TTGTCTGCTGGCAAAGTCTCACCTGAAACAGTTGACAGTGTGATTATGGGCAATGTCCTG
CAGAGTTCTTCAGATGCTATATATTTGGCAAGGCATGTTGGTTTGCGTGTGGGAATCCCA
AAGGAGACCCCAGCTCTCACGATTAATAGGCTCTGTGGTTCTGGTTTTCAGTCCATTGTG
AATGGATGTCAGGAAATTTGTGTTAAAGAAGCTGAAGTTGTTTTATGTGGAGGAACCGAA
AGCATGAGCCAAGCTCCCTACTGTGTCAGAAATGTGCGTTTTGGAACCAAGCTTGGATCA
GATATCAAGCTGGAAGATTCTTTATGGGTATCATTAACAGATCAGCATGTCCAGCTCCCC
ATGGCAATGACTGCAGAGAATCTTGCTGTAAAACACAAAATAAGCAGAGAAGAATGTGAC
AAATATGCCCTGCAGTCACAGCAGAGATGGAAAGCTGCTAATGATGCTGGCTACTTTAAT
GATGAAATGGCACCAATTGAAGTGAAGACAAAGAAAGGAAAACAGACAATGCAGGTAGAC
GAGCATGCTCGGCCCCAAACCACCCTGGAACAGTTACAGAAACTTCCTCCAGTATTCAAG
AAAGATGGAACTGTTACTGCAGGGAATGCATCGGGTGTAGCTGATGGTGCTGGAGCTGTT
ATCATAGCTAGTGAAGATGCTGTTAAGAAACATAACTTCACACCACTGGCAAGAATTGTG
GGCTACTTTGTATCTGGATGTGATCCCTCTATCATGGGTATTGGTCCTGTCCCTGCTATC
AGTGGGGCACTGAAGAAAGCAGGACTGAGTCTTAAGGACATGGATTTGGTAGAGGTGAAT
GAAGCTTTTGCTCCCCAGTACTTGGCTGTTGAGAGGAGTTTGGATCTTGACATAAGTAAA
ACCAATGTGAATGGAGGAGCCATTGCTTTGGGTCACCCACTGGGAGGATCTGGATCAAGA
ATTACTGCACACCTGGTTCACGAATTAAGGCGTCGAGGTGGAAAATATGCCGTTGGATCA
GCTTGCATTGGAGGTGGCCAAGGTATTGCTGTCATCATTCAGAGCACAGCCTGA
Enzyme 1 GenBank Gene ID BC001918 Link Image
Enzyme 1 GeneCard ID ACAA2 Link Image
Enzyme 1 GenAtlas ID ACAA2 Link Image
Enzyme 1 HGNC ID HGNC:83 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 18q21.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Abe H, Ohtake A, Yamamoto S, Satoh Y, Takayanagi M, Amaya Y, Takiguchi M, Sakuraba H, Suzuki Y, Mori M, et al.: Cloning and sequence analysis of a full length cDNA encoding human mitochondrial 3-oxoacyl-CoA thiolase. Biochim Biophys Acta. 1993 Nov 16;1216(2):304-6. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5277
Enzyme 2 Name Trifunctional enzyme subunit beta, mitochondrial
Enzyme 2 Synonyms
  1. TP-beta
  2. 3-ketoacyl-CoA thiolase
  3. Acetyl-CoA acyltransferase
  4. Beta-ketothiolase
Enzyme 2 Gene Name HADHB
Enzyme 2 Protein Sequence >Trifunctional enzyme subunit beta, mitochondrial
MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGV
RTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAA
LGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR
KLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLE
QDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPY
GTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATP
KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNW
GGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
Enzyme 2 Number of Residues 474
Enzyme 2 Molecular Weight 51294.0
Enzyme 2 Theoretical pI 9.94
Enzyme 2 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 2 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 2 Specific Function Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 2 Pathways
  • Benzoate Degradation via Hydroxylation (map00362 Link Image)
  • Bile Acid Biosynthesis (map00120 Link Image)
  • Fatty Acid Elongation In Mitochondria (map00062 Link Image)
  • Fatty Acid Metabolism (map00071 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 2 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID P55084 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ECHB_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1425 bp
ATGACTATCTTGACTTACCCCTTTAAAAATCTTCCCACTGCATCAAAATGGGCCCTCAGA
TTTTCCATAAGACCTCTGAGCTGTTCCTCCCAGCTACGAGCTGCCCCAGCTGTCCAGACC
AAAACGAAGAAGACGTTAGCCAAACCCAATATAAGGAATGTTGTGGTGGTGGATGGTGTT
CGCACTCCATTTTTGCTGTCTGGCACTTCATATAAAGACCTGATGCCACATGATTTGGCT
AGAGCAGCGCTTACGGGTTTGTTGCATCGGACCAGTGTCCCTAAGGAAGTAGTTGATTAT
ATCATCTTTGGTACAGTTATTCAGGAAGTGAAAACAAGCAATGTGGCTAGAGAGGCTGCC
CTTGGAGCTGGCTTCTCTGACAAGACTCCTGCTCACACTGTCACCATGGCTTGTATCTCT
GCCAACCAAGCCATGACCACAGGTGTTGGCTTGATTGCTTCTGGCCAGTGTGATGTGATC
GTGGCAGGTGGTGTTGAGTTGATGTCCGATGTCCCTATTCGTCACTCAAGGAAAATGAGA
AAACTGATGCTTGATCTCAATAAGGCCAAATCTATGGGCCAGCGACTGTCTTTAATCTCT
AAATTCCGATTTAATTTCCTAGCACCTGAGCTCCCTGCGGTTTCTGAGTTCTCCACCAGT
GAGACCATGGGCCACTCTGCAGACCGACTGGCCGCTGCCTTTGCTGTTTCTCGGCTGGAA
CAGGATGAATATGCACTGCGCTCTCACAGTCTAGCCAAGAAGGCACAGGATGAAGGACTC
CTTTCTGATGTGGTACCCTTCAAAGTACCAGGAAAAGATACAGTTACCAAAGATAATGGC
ATCCGTCCTTCCTCACTGGAGCAGATGGCCAAACTAAAACCTGCATTCATCAAGCCCTAC
GGCACAGTGACAGCTGCAAATTCTTCTTTCTTGACTGATGGTGCATCTGCAATGTTAATC
ATGGCGGAGGAAAAGGCTCTGGCCATGGGTTATAAGCCGAAGGCATATTTGAGGGATTTT
ATGTATGTGTCTCAGGATCCAAAAGATCAACTATTACTTGGACCAACATATGCTACTCCA
AAAGTTCTAGAAAAGGCAGGATTGACCATGAATGATATTGATGCTTTTGAATTTCATGAA
GCTTTCTCGGGTCAGATTTTGGCAAATTTTAAAGCCATGGATTCTGATTGGTTTGCAGAA
AACTACATGGGTAGAAAAACCAAGGTTGGATTGCCTCCTTTGGAGAAGTTTAATAACTGG
GGTGGATCTCTGTCCCTGGGACACCCATTTGGAGCCACTGGCTGCAGGTTGGTCATGGCT
GCTGCCAACAGATTACGGAAAGAAGGAGGCCAGTATGGCTTAGTGGCTGCGTGTGCAGCT
GGAGGGCAGGGCCATGCTATGATAGTGGAAGCTTATCCAAAATAA
Enzyme 2 GenBank Gene ID D16481 Link Image
Enzyme 2 GeneCard ID HADHB Link Image
Enzyme 2 GenAtlas ID HADHB Link Image
Enzyme 2 HGNC ID HGNC:4803 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2p23
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed Link Image]
  2. Orii KE, Aoyama T, Wakui K, Fukushima Y, Miyajima H, Yamaguchi S, Orii T, Kondo N, Hashimoto T: Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency. Hum Mol Genet. 1997 Aug;6(8):1215-24. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. Middleton B: The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase. Biochem Soc Trans. 1994 May;22(2):427-31. [PubMed Link Image]
  8. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  9. Kamijo T, Wanders RJ, Saudubray JM, Aoyama T, Komiyama A, Hashimoto T: Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients. J Clin Invest. 1994 Apr;93(4):1740-7. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  11. Ushikubo S, Aoyama T, Kamijo T, Wanders RJ, Rinaldo P, Vockley J, Hashimoto T: Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits. Am J Hum Genet. 1996 May;58(5):979-88. [PubMed Link Image]
  12. Spiekerkoetter U, Sun B, Khuchua Z, Bennett MJ, Strauss AW: Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to beta-subunit mutations. Hum Mutat. 2003 Jun;21(6):598-607. [PubMed Link Image]
  13. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5334
Enzyme 3 Name Long-chain specific acyl-CoA dehydrogenase, mitochondrial
Enzyme 3 Synonyms
  1. LCAD
Enzyme 3 Gene Name ACADL
Enzyme 3 Protein Sequence >Long-chain specific acyl-CoA dehydrogenase, mitochondrial
MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIF
RKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIV
WEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSD
LQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMK
GFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAI
SASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRL
DSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKE
LIAREIVFDK
Enzyme 3 Number of Residues 430
Enzyme 3 Molecular Weight 47655.3
Enzyme 3 Theoretical pI 7.89
Enzyme 3 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 3 Specific Function Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor
Enzyme 3 Pathways
Enzyme 3 Reactions
  • acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor [RN:R00392]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 177962 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P28330 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ACADL_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1293 bp
ATGGCCGCACGCCTTCTCCGAGGGTCCCTACGCGTCCTGGGCGGCCACCGTGCGCCGCGC
CAGCTGCCCGCCGCGCGATGTTCTCATTCCGGAGGGGAAGAACGTCTAGAAACTCCTTCT
GCTAAAAAATTAACAGATATAGGAATTCGAAGAATCTTTTCTCCAGAGCATGACATTTTC
CGGAAAAGTGTAAGGAAGTTTTTCCAAGAAGAAGTGATTCCTCATCACTCAGAATGGGAG
AAAGCTGGAGAAGTAAGTAGGGAGGTTTGGGAAAAAGCTGGAAAACAAGGACTGCTTGGT
GTCAATATTGCAGAGCATCTTGGTGGAATTGGAGGGGATCTGTACTCCGCAGCTATTGTC
TGGGAGGAGCAAGCTTATTCAAATTGTTCAGGCCCAGGTTTTAGTATTCATTCAGGTATT
GTCATGTCCTATATTACAAACCATGGCTCAGAAGAACAGATTAAGCACTTTATTCCCCAG
ATGACTGCAGGCAAATGTATTGGTGCAATAGCAATGACAGAGCCTGGAGCTGGAAGTGAC
TTACAGGGAATAAAAACAAATGCTAAAAAGGATGGAAGTGACTGGATTCTCAATGGAAGC
AAGGTGTTCATCAGTAATGGGTCATTAAGTGATGTTGTGATTGTAGTTGCGGTCACAAAT
CATGAAGCTCCCTCCCCTGCCCATGGTATTAGCCTTTTTCTGGTGGAAAATGGAATGAAA
GGATTTATCAAGGGACGAAAGCTACATAAAATGGGATTAAAAGCCCAGGATACCGCAGAA
CTATTCTTTGAAGATATACGGTTGCCAGCTAGTGCCCTACTTGGAGAAGAGAATAAAGGC
TTCTATTACATCATGAAAGAGCTTCCACAGGAAAGGCTGTTAATTGCTGATGTGGCAATT
TCAGCTAGTGAATTCATGTTTGAAGAAACCAGGAACTATGTTAAACAAAGAAAAGCTTTT
GGCAAAACAGTTGCTCACCTACAGACAGTGCAACATAAATTAGCAGAATTAAAAACACAT
ATATGTGTAACCCGAGCATTTGTGGACAACTGTCTCCAGCTGCATGAAGCGAAACGTTTG
GACTCCGCCACTGCTTGCATGGCGAAATATTGGGCATCTGAGTTACAAAATAGTGTAGCT
TACGACTGTGTACAGCTCCATGGAGGTTGGGGATACATGTGGGAGTACCCAATTGCAAAA
GCTTATGTGGATGCCAGAGTTCAGCCAATCTATGGTGGTACAAATGAAATAATGAAGGAG
CTGATTGCAAGAGAGATTGTCTTTGACAAGTAG
Enzyme 3 GenBank Gene ID M74096 Link Image
Enzyme 3 GeneCard ID ACADL Link Image
Enzyme 3 GenAtlas ID ACADL Link Image
Enzyme 3 HGNC ID HGNC:88 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2q34-q35
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Indo Y, Yang-Feng T, Glassberg R, Tanaka K: Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2. Genomics. 1991 Nov;11(3):609-20. [PubMed Link Image]
  2. Indo Y, Yang-Feng T, Glassberg R, Tanaka K: Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2. Genomics. 1992 Mar;12(3):626. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5336
Enzyme 4 Name Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Enzyme 4 Synonyms
  1. MCAD
Enzyme 4 Gene Name ACADM
Enzyme 4 Protein Sequence >Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEI
IPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ
TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKG
DEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNM
GQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEAT
KYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF
AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK
N
Enzyme 4 Number of Residues 421
Enzyme 4 Molecular Weight 46588.0
Enzyme 4 Theoretical pI 8.51
Enzyme 4 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 4 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 4 Specific Function This enzyme is specific for acyl chain lengths of 4 to 16
Enzyme 4 Pathways
Enzyme 4 Reactions
  • acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor [RN:R00392]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 177964 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P11310 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ACADM_HUMAN Link Image
Enzyme 4 PDB ID 1T9G Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1266 bp
ATGGCAGCGGGGTTCGGGCGATGCTGCAGGGTCCTGAGAAGTATTTCTCGTTTTCATTGG
AGATCACAGCATACAAAAGCCAATCGACAACGTGAACCAGGATTAGGATTTAGTTTTGAG
TTCACCGAACAGCAGAAAGAATTTCAAGCTACTGCTCGTAAATTTGCCAGAGAGGAAATC
ATCCCAGTGGCTGCAGAATATGATAAAACTGGTGAATATCCAGTCCCCCTAATTAGAAGA
GCCTGGGAACTTGGTTTAATGAACACACACATTCCAGAGAACTGTGGAGGTCTTGGACTT
GGAACTTTTGATGCTTGTTTAATTAGTGAAGAATTGGCTTATGGATGTACAGGGGTTCAG
ACTGCTATTGAAGGAAATTCTTTGGGGCAAATGCCTATTATTATTGCTGGAAATGATCAA
CAAAAGAAGAAGTATTTGGGGAGAATGACTGAGGAGCCATTGATGTGTGCTTATTGTGTA
ACAGAACCTGGAGCAGGCTCTGATGTAGCTGGTATAAAGACCAAAGCAGAAAAGAAAGGA
GATGAGTATATTATTAATGGTCAGAAGATGTGGATAACCAACGGAGGAAAAGCTAATTGG
TATTTTTTATTGGCACGTTCTGATCCAGATCCTAAAGCTCCTGCTAATAAAGCCTTTACT
GGATTCATTGTGGAAGCAGATACCCCAGGAATTCAGATTGGGAGAAAGGAATTAAACATG
GGCCAGCGATGTTCAGATACTAGAGGAATTGTCTTCGAAGATGTGAAAGTGCCTAAAGAA
AATGTTTTAATTGGTGACGGAGCTGGTTTCAAAGTTGCAATGGGAGCTTTTGATAAAACC
AGACCTGTAGTAGCTGCTGGTGCTGTTGGATTAGCACAAAGAGCTTTGGATGAAGCTACC
AAGTATGCCCTGGAAAGGAAAACTTTCGGAAAGCTACTTGTAGAGCACCAAGCAATATCA
TTTATGCTGGCTGAAATGGCAATGAAAGTTGAACTAGCTAGAATGAGTTACCAGAGAGCA
GCTTGGGAGGTTGATTCTGGTCGTCGAAATACCTATTATGCTTCTATTGCAAAGGCATTT
GCTGGAGATATTGCAAATCAGTTAGCTACTGATGCTGTGCAGATACTTGGAGGCAATGGA
TTTAATACAGAATATCCTGTAGAAAAACTAATGAGGGATGCCAAAATCTATCAGATTTAT
GAAGGTACTTCACAAATTCAAAGACTTATTGTAGCCCGTGAACACATTGACAAGTACAAA
AATTAA
Enzyme 4 GenBank Gene ID M16827 Link Image
Enzyme 4 GeneCard ID ACADM Link Image
Enzyme 4 GenAtlas ID ACADM Link Image
Enzyme 4 HGNC ID HGNC:89 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1p31
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Kelly DP, Kim JJ, Billadello JJ, Hainline BE, Chu TW, Strauss AW: Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue. Proc Natl Acad Sci U S A. 1987 Jun;84(12):4068-72. [PubMed Link Image]
  2. Zhang ZF, Kelly DP, Kim JJ, Zhou YQ, Ogden ML, Whelan AJ, Strauss AW: Structural organization and regulatory regions of the human medium-chain acyl-CoA dehydrogenase gene. Biochemistry. 1992 Jan 14;31(1):81-9. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Matsubara Y, Narisawa K, Miyabayashi S, Tada K, Coates PM, Bachmann C, Elsas LJ 2nd, Pollitt RJ, Rhead WJ, Roe CR: Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Biochem Biophys Res Commun. 1990 Aug 31;171(1):498-505. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity. Biochemistry. 1996 Sep 24;35(38):12412-20. [PubMed Link Image]
  9. Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D: Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex. J Biol Chem. 2004 Jul 30;279(31):32904-12. Epub 2004 May 24. [PubMed Link Image]
  10. Toogood HS, van Thiel A, Scrutton NS, Leys D: Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein. J Biol Chem. 2005 Aug 26;280(34):30361-6. Epub 2005 Jun 23. [PubMed Link Image]
  11. Tanaka K, Yokota I, Coates PM, Strauss AW, Kelly DP, Zhang Z, Gregersen N, Andresen BS, Matsubara Y, Curtis D, et al.: Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene. Hum Mutat. 1992;1(4):271-9. [PubMed Link Image]
  12. Yokota I, Indo Y, Coates PM, Tanaka K: Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation. J Clin Invest. 1990 Sep;86(3):1000-3. [PubMed Link Image]
  13. Kelly DP, Whelan AJ, Ogden ML, Alpers R, Zhang ZF, Bellus G, Gregersen N, Dorland L, Strauss AW: Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9236-40. [PubMed Link Image]
  14. Yokota I, Coates PM, Hale DE, Rinaldo P, Tanaka K: Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency. Am J Hum Genet. 1991 Dec;49(6):1280-91. [PubMed Link Image]
  15. Gregersen N, Andresen BS, Bross P, Winter V, Rudiger N, Engst S, Christensen E, Kelly D, Strauss AW, Kolvraa S, et al.: Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli. Hum Genet. 1991 Apr;86(6):545-51. [PubMed Link Image]
  16. Blakemore AI, Singleton H, Pollitt RJ, Engel PC, Kolvraa S, Gregersen N, Curtis D: Frequency of the G985 MCAD mutation in the general population. Lancet. 1991 Feb 2;337(8736):298-9. [PubMed Link Image]
  17. Andresen BS, Jensen TG, Bross P, Knudsen I, Winter V, Kolvraa S, Bolund L, Ding JH, Chen YT, Van Hove JL, et al.: Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene. Am J Hum Genet. 1994 Jun;54(6):975-88. [PubMed Link Image]
  18. Ziadeh R, Hoffman EP, Finegold DN, Hoop RC, Brackett JC, Strauss AW, Naylor EW: Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies. Pediatr Res. 1995 May;37(5):675-8. [PubMed Link Image]
  19. Brackett JC, Sims HF, Steiner RD, Nunge M, Zimmerman EM, deMartinville B, Rinaldo P, Slaugh R, Strauss AW: A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death. J Clin Invest. 1994 Oct;94(4):1477-83. [PubMed Link Image]
  20. Andresen BS, Bross P, Udvari S, Kirk J, Gray G, Kmoch S, Chamoles N, Knudsen I, Winter V, Wilcken B, Yokota I, Hart K, Packman S, Harpey JP, Saudubray JM, Hale DE, Bolund L, Kolvraa S, Gregersen N: The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype? Hum Mol Genet. 1997 May;6(5):695-707. [PubMed Link Image]
  21. Kuchler B, Abdel-Ghany AG, Bross P, Nandy A, Rasched I, Ghisla S: Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site. Biochem J. 1999 Jan 15;337 ( Pt 2):225-30. [PubMed Link Image]
  22. Yang BZ, Ding JH, Zhou C, Dimachkie MM, Sweetman L, Dasouki MJ, Wilkinson J, Roe CR: Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Mol Genet Metab. 2000 Mar;69(3):259-62. [PubMed Link Image]
  23. Andresen BS, Dobrowolski SF, O'Reilly L, Muenzer J, McCandless SE, Frazier DM, Udvari S, Bross P, Knudsen I, Banas R, Chace DH, Engel P, Naylor EW, Gregersen N: Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency. Am J Hum Genet. 2001 Jun;68(6):1408-18. Epub 2001 May 8. [PubMed Link Image]
  24. Zschocke J, Schulze A, Lindner M, Fiesel S, Olgemoller K, Hoffmann GF, Penzien J, Ruiter JP, Wanders RJ, Mayatepek E: Molecular and functional characterisation of mild MCAD deficiency. Hum Genet. 2001 May;108(5):404-8. [PubMed Link Image]
  25. Albers S, Levy HL, Irons M, Strauss AW, Marsden D: Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency. J Inherit Metab Dis. 2001 Jun;24(3):417-8. [PubMed Link Image]
  26. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5378
Enzyme 5 Name Peroxisomal acyl-coenzyme A oxidase 1
Enzyme 5 Synonyms
  1. AOX
  2. Palmitoyl-CoA oxidase
  3. Straight-chain acyl-CoA oxidase
  4. SCOX
Enzyme 5 Gene Name ACOX1
Enzyme 5 Protein Sequence >Peroxisomal acyl-coenzyme A oxidase 1
MNPDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRY
EVAVRKSAIMVKKMREFGIADPDEIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQK
EKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGL
GKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYL
KMDNHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIA
IRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIG
QGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTF
EGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPTMVDINSP
ESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFS
EKLLKIQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIR
SDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKNSPLNKAEVHESYKHLKSLQSKL
Enzyme 5 Number of Residues 660
Enzyme 5 Molecular Weight 74423.0
Enzyme 5 Theoretical pI 8.29
Enzyme 5 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleoside binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 5 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 5 Specific Function Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs
Enzyme 5 Pathways
Enzyme 5 Reactions
  • acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 14250616 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q15067 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ACOX1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1983 bp
ATGAACCCGGACCTGCGCAGGGAGCGGGATTCCGCCAGCTTCAACCCGGAGCTGCTTACA
CACATCCTGGACGGCAGCCCCGAGAAAACCCGGCGCCGCCGAGAGATCGAGAACATGATC
CTGAACGACCCAGACTTCCAGCATGAGGACTTGAACTTCCTCACTCGCAGCCAGCGTTAT
GAGGTGGCTGTCAGGAAAAGTGCCATCATGGTGAAGAAGATGAGGGAGTTTGGCATCGCT
GACCCTGATGAAATTATGTGGTTTAAAAATTTTGTGCACCGAGGGCGGCCTGAGCCTCTG
GATCTTCACTTGGGCATGTTCCTGCCCACCTTGCTTCACCAGGCAACTGCGGAGCAGCAG
GAGCGCTTCTTCATGCCCGCCTGGAACTTGGAGATCATTGGCACTTATGCCCAGACAGAG
ATGGGTCATGGAACTCACCTTCGAGGCTTGGAAACCACAGCCACGTATGACCCTGAAACC
CAGGAGTTCATTCTCAACAGTCCTACTGTGACCTCCATTAAATGGTGGCCTGGTGGGCTT
GGAAAGACTTCAAATCATGCAATAGTTCTTGCCCAGCTCATCACTAAGGGGAAATGCTAT
GGATTACATGCCTTTATCGTACCTATTCGTGAAATCGGGACCCATAAGCCTTTGCCAGGA
ATTACCGTTGGTGACATCGGCCCCAAATTTGGTTATGATGAGATAGACAATGGCTACCTC
AAAATGGACAACCATCGTATTCCCAGAGAAAACATGCTGATGAAGTATGCCCAGGTGAAG
CCTGATGGCACATACGTGAAACCGCTGAGTAACAAGCTGACTTACGGGACCATGGTGTTT
GTCAGGTCCTTCCTTGTGGGAGAAGCTGCTCGGGCTCTGTCTAAGGCGTGCACCATTGCC
ATCCGATACAGCGCTGTGAGGCACCAGTCTGAAATGAAGCCAGGTGAACCAGAACCACAG
ATTTTGGATTTTCAAACCCAGCAGTATAAACTCTTTCCACTCCTGGCCACTGCCTATGCC
TTCCAGTTTGTGGGCGCATACATGAAGGAGACCTATCACCGGATTAACGAAGGCATTGGT
CAAGGGGACCTGAGTGAACTGCCTGAGCTTCATGCCCTCACCGCTGGACTGAAGGCTTTC
ACCTCCTGGACTGCAAACACTGGCATTGAAGCATGTCGGATGGCTTGTGGTGGGCATGGC
TATTCTCATTGCAGTGGTCTTCCAAATATTTATGTCAATTTCACCCCAAGCTGTACCTTT
GAGGGAGAAAACACTGTCATGATGCTCCAGACGGCTAGGTTCCTGATGAAAAGTTATGAT
CAGGTGCACTCAGGAAAGTTGGTGTGTGGCATGGTGTCCTATTTGAACGACCTGCCCAGT
CAGCGCATCCAGCCACAGCAGGTAGCAGTCTGGCCAACCATGGTGGATATCAACAGCCCC
GAAAGCCTAACCGAAGCATATAAACTCCGTGCAGCCAGATTAGTAGAAATTGCTGCAAAA
AACCTTCAAAAAGAAGTGATTCACAGAAAAAGCAAGGAGGTAGCTTGGAACCTAACTTCT
GTTGACCTTGTTCGAGCAAGTGAGGCACATTGCCACTATGTGGTAGTTAAGCTCTTTTCA
GAAAAACTCCTCAAAATTCAAGATAAAGCCATTCAAGCTGTCTTAAGGAGTTTATGTCTG
CTGTATTCTCTGTATGGAATCAGTCAGAACGCGGGGGATTTCCTTCAGGGGAGCATCATG
ACAGAGCCTCAGATTACACAAGTAAACCAGCGTGTAAAGGAGTTACTCACTCTGATTCGC
TCAGATGCTGTTGCTTTGGTTGATGCATTTGATTTTCAGGATGTGACACTTGGCTCTGTG
CTTGGCCGCTATGATGGGAATGTGTATGAAAACTTGTTTGAGTGGGCTAAGAACTCCCCA
CTGAACAAAGCAGAGGTCCACGAATCTTACAAGCACCTGAAGTCACTGCAGTCCAAGCTC
TGA
Enzyme 5 GenBank Gene ID BC008767 Link Image
Enzyme 5 GeneCard ID ACOX1 Link Image
Enzyme 5 GenAtlas ID ACOX1 Link Image
Enzyme 5 HGNC ID HGNC:119 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 17q24-q25|17q25.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK: Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3107-11. [PubMed Link Image]
  2. Chu R, Varanasi U, Chu S, Lin Y, Usuda N, Rao MS, Reddy JK: Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells. J Biol Chem. 1995 Mar 3;270(9):4908-15. [PubMed Link Image]
  3. Fournier B, Saudubray JM, Benichou B, Lyonnet S, Munnich A, Clevers H, Poll-The BT: Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy. J Clin Invest. 1994 Aug;94(2):526-31. [PubMed Link Image]
  4. Aoyama T, Tsushima K, Souri M, Kamijo T, Suzuki Y, Shimozawa N, Orii T, Hashimoto T: Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1113-8. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Suzuki Y, Iai M, Kamei A, Tanabe Y, Chida S, Yamaguchi S, Zhang Z, Takemoto Y, Shimozawa N, Kondo N: Peroxisomal acyl CoA oxidase deficiency. J Pediatr. 2002 Jan;140(1):128-30. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5424
Enzyme 6 Name Peroxisomal acyl-coenzyme A oxidase 3
Enzyme 6 Synonyms
  1. Branched-chain acyl-CoA oxidase
  2. BRCACox
  3. Pristanoyl-CoA oxidase
Enzyme 6 Gene Name ACOX3
Enzyme 6 Protein Sequence >Peroxisomal acyl-coenzyme A oxidase 3
MASTVEGGDTALLPEFPRGPLDAYRARASFSWKELALFTEGEGMLRFKKTIFSALENDPL
FARSPGADLSLEKYRELNFLRCKRIFEYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAK
YLLHSLVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPAT
EEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQCHGLHPFIVQIRDPKTLLPMP
GVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGAS
LGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYL
AAVYALDHFSKSLFLDLVELQRGLASGDRSARQAELGREIHALASASKPLASWTTQQGIQ
ECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHDGACFR
SPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYKWLVCYLLRETYQKLNQEKRSG
SSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWSL
SRHAALLYRGGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADG
ELYKNLWGAVLQESKVLERASWWPEFSVNKPVIGSLKSKL
Enzyme 6 Number of Residues 700
Enzyme 6 Molecular Weight 77628.3
Enzyme 6 Theoretical pI 7.27
Enzyme 6 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleoside binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 6 General Function Involved in oxidoreductase activity, acting on the CH-CH group of donors
Enzyme 6 Specific Function Oxidizes the CoA-esters of 2-methyl-branched fatty acids
Enzyme 6 Pathways
Enzyme 6 Reactions
  • acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 2326549 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O15254 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ACOX3_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2103 bp
ATGGCATCCACTGTGGAAGGAGGCGACACAGCTCTGCTCCCAGAATTCCCCAGGGGGCCC
CTCGATGCCTACCGAGCAAGAGCGTCCTTCAGCTGGAAGGACGTGGCGCTGTTCACGGAA
GGGGAGGGCAATGTCCGCTTTAAGAAAACCATCTTCTCAGCTCTTGAGAATGACCCTCTT
TTCGCTCGTTCCCCTGGAGCCGACCTGTCCTTGGAGAAGTATCGCGAGCTGAACTTCCTT
CGATGCAAGCGGATCTTCGAGTATGACTTCCTCAGTGTCGAAGCAATGTTCAAGAGCCCT
CTGAAGGTCCCCGCCTTGATTCAGTGCCTGGGCATGTATGACTCTTCTCTGGCTGCCAAG
TACCTCCTCCATAGCTTGGTTTTTGGATCAGCAGTTTACAGTTCTGGTTCTGAAAGACAT
CTCACATATATTCAAAAGATCTTCAGGATGGAGATTTTTGGATGTTTTGCTCTGACCGAA
TTAAGCCACGGCAGTAATACCAAGGCCATTCGCACAACTGCCCACTACGATCCTGCCACT
GAGGAATTCATCATACATTCCCCTGATTTCGAAGCTGCCAAGTTTTGGGTTGGCAACATG
GGCAAGACAGCCACTCACGCGGTGGTGTTTGCTAAGCTGTGTGTGCCAGGGGACCAGTGC
CATGGGCTGCATCCCTTTATCGTGCAGATCCGGGACCCGAAGACCCTTCTTCCCATGCCT
GGAGTGATGGTTGGCGACATAGGAAAAAAACTCGGGCAGAACGGTCTAGATAATGGTTTC
GCCATGTTCCACAAGGTCAGAGTTCCTCGCCAGAGCCTTCTGAACCGGATGGGAGACGTC
ACCCCCGAGGGCACCTATGTCAGCCCCTTTAAGGACGTCAGGCAGCGCTTTGGAGCGTCC
CTGGGGAGCCTGTCCTCGGGCCGGGTCTCCATCGTGAGCCTGGCCATCCTTAACCTAAAG
CTGGCCGTGGCCATCGCTCTTCGCTTCTCAGCCACTCGGCGTCAGTTTGGACCCACAGAG
GAGGAGGAAATACCAGTGCTTGAGTATCCAATGCAGCAATGGCGCTTGCTTCCATATCTG
GCAGCTGTCTACGGCTTAGACCATTTCTCCAAGTCGCTCTTCCTGGACCTGGTGGAGCTC
CAGCGAGGACTTGCATCGGGAGACCGCAGCGCCAGACAGGCAGAGCTTGGACGTGAGATC
CACGCCCTGGCATCGGCCAGCAAGCCCCTGGCCTCGTGGACCACCCAGCAAGGAATTCAG
GAATGCCGGGAGGCGTGTGGAGGACACGGCTATCTGGCCATGAACCGGTTGGGTGTCCTT
AGAGATGACAACGATCCCAACTGCACATACGAAGGTGACAACAACATCCTGCTGCAGCAG
ACAAGCAACTATTTGCTGGGTCTCCTGGCACACCAGGTCCACGATGGAGCTTGCTTCCGC
AGTCCGCTGAAGTCAGTGGACTTTCTGGACGCCTATCCCGGCATCCTTGACCAGAAGTTT
GAGGTCTCCAGTGTTGCCGACTGCTTGGACTCTGCAGTCGCCCTGGCAGCATACAAGTGG
CTGGTTTGCTACCTGCTCCGAGAGACTTATCAAAAATTAAACCAAGAGAAAAGATCAGGA
AGCAGTGACTTTGAAGCAAGGAACAAATGCCAGGTGTCCCACGGCCGTCCGTTGGCGCTG
GCCTTCGTGGAGCTCACGGTGGTCCAGAGGTTCCACGAGCACGTGCACCAGCCTTCCGTG
CCGCCCTCGCTGCGGGCCGTGCTGGGGCGGCTCAGTGCTCTGTACGCCCTGTGGTCCCTG
AAGCGCCACGCGGCCCTGCTCTACCGAGGAGGATACTTCTCCGGTGAGCAGGCGGGAGAA
GTGTTGGAGAGCGCCGTCCTGGCTTTGTGTTCCCAGCTGAAAGACGATGCAGTTGCCCTG
GTAGACGTGATCGCTCCTCCTGACTTTGTTCTGGACTCACCGATTGGCAGAGCCGACGGC
GAGCTCTACAAAAACCTCTGGGGCGCTGTCCTGCAGGAAAGCAAGGTGTTGGAGCGGGCA
TCCTGGTGGCCAGAGTTTTCTGTGAACAAACCTGTCATAGGAAGTCTGAAATCGAAGCTC
TAG
Enzyme 6 GenBank Gene ID Y11411 Link Image
Enzyme 6 GeneCard ID ACOX3 Link Image
Enzyme 6 GenAtlas ID ACOX3 Link Image
Enzyme 6 HGNC ID HGNC:121 Link Image
Enzyme 6 Chromosome Location 4
Enzyme 6 Locus 4p15.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Vanhooren JC, Marynen P, Mannaerts GP, Van Veldhoven PP: Evidence for the existence of a pristanoyl-CoA oxidase gene in man. Biochem J. 1997 Aug 1;325 ( Pt 3):593-9. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6299
Enzyme 7 Name Peroxisomal trans-2-enoyl-CoA reductase
Enzyme 7 Synonyms
  1. TERP
  2. 2,4-dienoyl-CoA reductase-related protein
  3. DCR-RP
  4. HPDHase
  5. pVI-ARL
Enzyme 7 Gene Name PECR
Enzyme 7 Protein Sequence >Peroxisomal trans-2-enoyl-CoA reductase
MASWAKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAAD
ELQANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHIS
SKGWHAVLETNLTGTFYMCKAVYSSWMKEHGGSIVNIIVPTKAGFPLAVHSGAARAGVYN
LTKSLALEWACSGIRINCVAPGVIYSQTAVENYGSWGQSFFEGSFQKIPAKRIGVPEEVS
SVVCFLLSPAASFITGQSVDVDGGRSLYTHSYEVPDHDNWPKGAGDLSVVKKMKETFKEK
AKL
Enzyme 7 Number of Residues 303
Enzyme 7 Molecular Weight 32544.1
Enzyme 7 Theoretical pI 9.12
Enzyme 7 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • biological regulation
  • metabolic process
  • oxidation reduction
  • regulation of apoptosis
  • regulation of biological process
  • regulation of cell death
  • regulation of cellular process
  • regulation of programmed cell death
Component
Enzyme 7 General Function Involved in regulation of apoptosis
Enzyme 7 Specific Function Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+ [RN:R07162]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID Q9BY49 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PECR_HUMAN Link Image
Enzyme 7 PDB ID 1YXM Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >912 bp
ATGGCCTCCTGGGCTAAGGGCAGGAGCTACCTGGCGCCTGGTTTGCTGCAGGGCCAAGTG
GCCATCGTCACCGGCGGGGCCACGGGCATCGGAAAAGCCATCGTGAAGGAGCTCCTGGAG
CTGGGGAGTAATGTGGTCATTGCATCCCGTAAGTTGGAGAGATTGAAGTCTGCGGCAGAT
GAACTGCAGGCCAACCTACCTCCCACAAAGCAGGCACGAGTCATTCCCATACAATGCAAC
ATCCGGAATGAGGAGGAGGTGAATAATTTGGTCAAATCTACCTTAGATACTTTTGGTAAG
ATCAATTTCTTGGTGAACAATGGAGGAGGCCAGTTTCTTTCCCCTGCTGAACACATCAGT
TCTAAGGGATGGCACGCTGTGCTTGAGACCAACCTGACGGGTACCTTCTACATGTGCAAA
GCAGTTTACAGCTCCTGGATGAAAGAGCATGGAGGATCTATCGTCAATATCATTGTCCCT
ACTAAAGCTGGATTTCCATTAGCTGTGCATTCTGGAGCTGCAAGAGCAGGTGTTTACAAC
CTCACCAAATCTTTAGCTTTGGAATGGGCCTGCAGTGGAATACGGATCAATTGTGTTGCC
CCTGGAGTTATTTATTCCCAGACTGCTGTGGAGAACTATGGTTCCTGGGGACAAAGCTTC
TTTGAAGGGTCTTTTCAGAAAATCCCCGCTAAACGAATTGGTGTTCCTGAGGAGGTCTCC
TCTGTGGTCTGCTTCCTACTGTCTCCTGCAGCTTCCTTCATCACTGGACAGTCAGTGGAT
GTGGATGGGGGCCGGAGTCTCTATACTCACTCGTATGAGGTACCAGATCATGACAACTGG
CCCAAGGGAGCAGGGGACCTTTCTGTTGTCAAAAAGATGAAGGAGACCTTTAAGGAGAAA
GCTAAGCTCTGA
Enzyme 7 GenBank Gene ID AF232009 Link Image
Enzyme 7 GeneCard ID PECR Link Image
Enzyme 7 GenAtlas ID PECR Link Image
Enzyme 7 HGNC ID HGNC:18281 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 2q35
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Das AK, Uhler MD, Hajra AK: Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs. J Biol Chem. 2000 Aug 11;275(32):24333-40. [PubMed Link Image]
  2. Amery L, Mannaerts GP, Subramani S, Van Veldhoven PP, Fransen M: Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology. Comb Chem High Throughput Screen. 2001 Nov;4(7):545-52. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Braastad CD, Leguia M, Hendrickson EA: Ku86 autoantigen related protein-1 transcription initiates from a CpG island and is induced by p53 through a nearby p53 response element. Nucleic Acids Res. 2002 Apr 15;30(8):1713-24. [PubMed Link Image]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6874
Enzyme 8 Name Glycylpeptide N-tetradecanoyltransferase 1
Enzyme 8 Synonyms
  1. Myristoyl-CoA:protein N-myristoyltransferase 1
  2. NMT 1
  3. Type I N-myristoyltransferase
  4. Peptide N-myristoyltransferase 1
Enzyme 8 Gene Name NMT1
Enzyme 8 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 1
MADESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKK
QKKKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFW
DTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENY
VEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEK
KMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRS
LNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQF
HLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAY
SFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYN
WKCPSMGAEKVGLVLQ
Enzyme 8 Number of Residues 496
Enzyme 8 Molecular Weight 56805.9
Enzyme 8 Theoretical pI 7.91
Enzyme 8 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • N-terminal protein lipidation
  • N-terminal protein myristoylation
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
Enzyme 8 General Function Involved in glycylpeptide N-tetradecanoyltransferase activity
Enzyme 8 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide [RN:R03992]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID P30419 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NMT1_HUMAN Link Image
Enzyme 8 PDB ID 1RXT Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1491 bp
ATGGCGGACGAGAGTGAGACAGCAGTGAAGCCGCCGGCACCTCCGCTGCCGCAGATGATG
GAAGGGAACGGGAACGGCCATGAGCACTGCAGCGATTGCGAGAATGAGGAGGACAACAGC
TACAACCGGGGTGGTTTGAGTCCAGCCAATGACACTGGAGCCAAAAAGAAGAAAAAGAAA
CAAAAAAAGAAGAAAGAAAAAGGCAGTGAGACAGATTCAGCCCAGGATCAGCCTGTGAAG
ATGAACTCTTTGCCAGCAGAGAGGATCCAGGAAATACAGAAGGCCATTGAGCTGTTCTCA
GTGGGTCAGGGACCTGCCAAAACCATGGAGGAGGCTAGCAAGCGAAGCTACCAGTTCTGG
GATACGCAGCCCGTCCCCAAGCTGGGCGAAGTGGTGAACACCCATGGCCCCGTGGAGCCT
GACAAGGACAATATCCGCCAGGAGCCCTACACCCTGCCCCAGGGCTTCACCTGGGATGCT
TTGGACTTGGGCGATCGTGGTGTGCTAAAAGAACTGTACACCCTCCTGAATGAGAACTAT
GTGGAAGATGATGACAACATGTTCCGATTTGATTATTCCCCGGAGTTTCTTTTGTGGGCT
CTCCGGCCACCCGGCTGGCTCCCCCAGTGGCACTGTGGGGTTCGAGTGGTCTCAAGTCGG
AAATTGGTTGGGTTCATTAGCGCCATCCCAGCAAACATCCATATCTATGACACAGAGAAG
AAGATGGTAGAGATCAACTTCCTGTGTGTCCACAAGAAGCTGCGTTCCAAGAGGGTTGCT
CCAGTTCTGATCCGAGAGATCACCAGGCGGGTTCACCTGGAGGGCATCTTCCAAGCAGTT
TACACTGCCGGGGTGGTACTACCAAAGCCCGTTGGCACCTGCAGGTATTGGCATCGGTCC
CTAAACCCACGGAAGCTGATTGAAGTGAAGTTCTCCCACCTGAGCAGAAATATGACCATG
CAGCGCACCATGAAGCTCTACCGACTGCCAGAGACTCCCAAGACAGCTGGGCTGCGACCA
ATGGAAACAAAGGACATTCCAGTAGTGCACCAGCTCCTCACCAGGTACTTGAAGCAATTT
CACCTTACGCCCGTCATGAGCCAGGAGGAGGTGGAGCACTGGTTCTACCCCCAGGAGAAT
ATCATCGACACTTTCGTGGTGGAGAACGCAAACGGAGAGGTGACAGATTTCCTGAGCTTT
TATACGCTGCCCTCCACCATCATGAACCATCCAACCCACAAGAGTCTCAAAGCTGCTTAT
TCTTTCTACAACGTTCACACCCAGACCCCTCTTCTAGACCTCATGAGCGACGCCCTTGTC
CTCGCCAAAATGAAAGGGTTTGATGTGTTCAATGCACTGGATCTCATGGAGAACAAAACC
TTCCTGGAGAAGCTCAAGTTTGGCATAGGGGACGGCAACCTGCAGTATTACCTTTACAAT
TGGAAATGCCCCAGCATGGGGGCAGAGAAGGTTGGACTGGTGCTACAATAA
Enzyme 8 GenBank Gene ID AF043324 Link Image
Enzyme 8 GeneCard ID NMT1 Link Image
Enzyme 8 GenAtlas ID NMT1 Link Image
Enzyme 8 HGNC ID HGNC:7857 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 17q21.31
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Glover CJ, Hartman KD, Felsted RL: Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction. J Biol Chem. 1997 Nov 7;272(45):28680-9. [PubMed Link Image]
  2. Giang DK, Cravatt BF: A second mammalian N-myristoyltransferase. J Biol Chem. 1998 Mar 20;273(12):6595-8. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Duronio RJ, Reed SI, Gordon JI: Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1992 May 1;89(9):4129-33. [PubMed Link Image]
  6. McIlhinney RA, Young K, Egerton M, Camble R, White A, Soloviev M: Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme. Biochem J. 1998 Aug 1;333 ( Pt 3):491-5. [PubMed Link Image]
  7. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  8. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  9. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  10. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  11. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  12. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  13. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  14. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6876
Enzyme 9 Name Glycylpeptide N-tetradecanoyltransferase 2
Enzyme 9 Synonyms
  1. Myristoyl-CoA:protein N-myristoyltransferase 2
  2. NMT 2
  3. Peptide N-myristoyltransferase 2
  4. Type II N-myristoyltransferase
Enzyme 9 Gene Name NMT2
Enzyme 9 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 2
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPN
SGGTKSDSASDSQEIKIQQPSKNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQ
FWDTQPVPKLDEVITSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNE
NYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDS
VKKMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWH
RSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLK
QFHLAPVMDEEEVAHWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKA
AYSFYNIHTETPLLDLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYL
YNWRCPGTDSEKVGLVLQ
Enzyme 9 Number of Residues 498
Enzyme 9 Molecular Weight 56979.8
Enzyme 9 Theoretical pI 7.65
Enzyme 9 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • N-terminal protein lipidation
  • N-terminal protein myristoylation
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
Enzyme 9 General Function Involved in glycylpeptide N-tetradecanoyltransferase activity
Enzyme 9 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide [RN:R03992]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 3005065 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O60551 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name NMT2_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1497 bp
ATGGCGGAGGACAGCGAGTCTGCGGCCAGCCAGCAGAGCCTGGAACTGGACGACCAGGAC
ACGTGCGGGATAGACGGGGACAATGAGGAGGAGACGGAGCACGCCAAAGGAAGTCCTGGA
GGGTATTTGGGAGCCAAAAAGAAAAAGAAGAAACAGAAGAGAAAAAAGGAGAAACCAAAT
TCCGGAGGCACCAAGTCAGACTCGGCATCTGATTCCCAGGAGATTAAAATTCAGCAGCCT
TCGAAAAATCCCAGTGTTCCAATGCAGAAGTTGCAGGATATCCAGAGAGCAATGGAGCTG
CTATCCGCATGCCAGGGCCCAGCCAGGAACATTGATGAGGCTGCAAAGCACAGATACCAG
TTTTGGGACACACAACCGGTACCAAAACTAGATGAAGTCATAACATCTCATGGTGCAATT
GAACCAGATAAAGACAACGTACGCCAAGAACCGTATTCTTTGCCACAGGGTTTTATGTGG
GACACTTTAGACTTGAGTGATGCCGAAGTGCTCAAGGAGTTATACACGTTGTTAAATGAG
AATTACGTAGAAGATGATGACAATATGTTCCGATTTGACTATTCACCCGAGTTCCTGTTG
TGGGCTCTGCGTCCACCAGGCTGGCTCCTGCAGTGGCACTGTGGGGTCAGAGTGTCTTCA
AATAAAAAACTGGTCGGGTTCATAAGTGCCATCCCAGCAAACATTCGGATTTATGACAGT
GTGAAGAAGATGGTAGAAATCAACTTTCTTTGTGTTCATAAGAAGTTGAGATCGAAACGG
GTAGCCCCAGTGCTAATCCGAGAGATCACTAGAAGAGTGAACCTGGAAGGGATCTTCCAG
GCTGTGTACACCGCGGGAGTGGTTCTTCCTAAGCCCATAGCCACATGCAGATACTGGCAT
CGATCACTAAACCCCAGAAAATTGGTAGAAGTGAAATTTTCTCACTTGAGTAGAAATATG
ACTTTACAGAGAACAATGAAGCTATACAGACTTCCAGATGTTACAAAGACTTCAGGTTTG
AGACCAATGGAACCAAAAGATATCAAATCAGTTCGAGAATTAATCAACACTTACCTGAAG
CAGTTTCATCTGGCTCCAGTGATGGATGAAGAGGAAGTAGCCCACTGGTTCCTCCCCCGG
GAGCACATTATTGACACGTTTGTAGTGGAGAGCCCCAACGGTAAACTGACTGATTTCCTG
AGCTTCTATACGCTCCCCTCCACGGTGATGCACCACCCTGCTCACAAGAGCCTCAAAGCC
GCCTACTCATTCTACAACATCCACACAGAGACGCCCCTGCTGGACCTCATGAGCGACGCG
CTCATCCTGGCTAAATCGAAAGGATTTGATGTATTCAATGCACTGGATTTGATGGAAAAT
AAGACATTCTTGGAAAAACTCAAGTTTGGTATAGGAGATGGCAATTTGCAGTATTACCTG
TACAATTGGAGGTGTCCAGGTACAGATTCTGAAAAGGTTGGACTAGTACTACAATAG
Enzyme 9 GenBank Gene ID AF043325 Link Image
Enzyme 9 GeneCard ID NMT2 Link Image
Enzyme 9 GenAtlas ID NMT2 Link Image
Enzyme 9 HGNC ID HGNC:7858 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 10p13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Giang DK, Cravatt BF: A second mammalian N-myristoyltransferase. J Biol Chem. 1998 Mar 20;273(12):6595-8. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 13023
Enzyme 10 Name Acyl-Coenzyme A dehydrogenase, long chain
Enzyme 10 Synonyms
  1. Putative uncharacterized protein ACADL
Enzyme 10 Gene Name ACADL
Enzyme 10 Protein Sequence >Acyl-Coenzyme A dehydrogenase, long chain
MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIF
RKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIV
WEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSD
LQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMK
GFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAI
SASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRL
DSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKE
LIAREIVFDK
Enzyme 10 Number of Residues 430
Enzyme 10 Molecular Weight 47656
Enzyme 10 Theoretical pI 7.89
Enzyme 10 GO Classification
Function
  • acyl-CoA dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 10 General Function Lipid transport and metabolism
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 24660234 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q8IUN8 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name Q8IUN8_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID BC039063 Link Image
Enzyme 10 GeneCard ID Q8IUN8 Link Image
Enzyme 10 GenAtlas ID ACADL Link Image
Enzyme 10 HGNC ID HGNC:88 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 15876
Enzyme 11 Name ACAA1 protein
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name ACAA1
Enzyme 11 Protein Sequence >ACAA1 protein
MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTT
PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVN
RQCSSGLQAVASIAGGIRNGSYDIGMACGITSENVAERFGISREKQDTFALASQQKAARA
QSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAG
LTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQAITLLNE
LKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN
Enzyme 11 Number of Residues 331
Enzyme 11 Molecular Weight 34636.4
Enzyme 11 Theoretical pI 8.49
Enzyme 11 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 11 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 15680239 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q96CA6 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name Q96CA6_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >996 bp
ATGCAGAGGCTGCAGGTAGTGCTGGGCCACCTGAGGGGTCCGGCCGATTCCGGCTGGATG
CCGCAGGCCGCGCCTTGCCTGAGCGGTGCCCCGCAGGCCTCGGCCGCGGACGTGGTGGTG
GTGCACGGGCGGCGCACGGCCATCTGCCGGGCGGGCCGCGGCGGCTTCAAGGACACCACC
CCCGACGAGCTTCTCTCGGCAGTCATGACCGCGGTTCTCAAGGACGTGAATCTGAGGCCG
GAACAGCTGGGGGACATCTGTGTCGGAAATGTGCTGCAGCCTGGGGCCGGGGCAATCATG
GCCCGAATCGCCCAGTTTCTGAGTGACATCCCGGAGACTGTGCCTTTGTCCACTGTCAAT
AGACAGTGTTCGTCGGGGCTACAGGCAGTGGCCAGCATAGCAGGTGGCATCAGAAATGGG
TCTTATGACATTGGCATGGCCTGTGGGATAACCTCTGAGAATGTGGCTGAGCGGTTTGGC
ATTTCACGGGAGAAGCAGGATACCTTTGCCCTGGCTTCCCAGCAGAAGGCAGCAAGAGCC
CAGAGCAAGGGCTGTTTCCAAGCTGAGATTGTGCCTGTGACCACCACGGTCCATGATGAC
AAGGGCACCAAGAGGAGCATCACTGTGACCCAGGATGAGGGTATCCGCCCCAGCACCACC
ATGGAGGGCCTGGCCAAACTGAAGCCTGCCTTCAAGAAAGATGGTTCTACCACAGCTGGG
CTGACAGTGAGTGACGTGGACATCTTCGAGATCAATGAGGCCTTTGCAAGCCAGGCTGCC
TACTGTGTGGAGAAGCTACGACTCCCCCCTGAGAAGGTGAACCCCCTGGGGGGTGCAGTG
GCCTTAGGGCACCCACTGGGCTGCACTGGGGCACGACAGGCCATCACGCTGCTCAATGAG
CTGAAGCGCCGTGGGAAGAGGGCATACGGAGTGGTGTCCATGTGCATCGGGACTGGAATG
GGAGCCGCTGCCGTCTTTGAATACCCTGGGAACTGA
Enzyme 11 GenBank Gene ID BC014474 Link Image
Enzyme 11 GeneCard ID ACAA1 Link Image
Enzyme 11 GenAtlas ID ACAA1 Link Image
Enzyme 11 HGNC ID HGNC:82 Link Image
Enzyme 11 Chromosome Location 3
Enzyme 11 Locus 3p23-p22
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16031
Enzyme 12 Name cDNA FLJ76905, highly similar to Homo sapiens N-myristoyltransferase 1 (NMT1), mRNA (N-myristoyltransferase 1, isoform CRA_b)
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name NMT1
Enzyme 12 Protein Sequence >cDNA FLJ76905, highly similar to Homo sapiens N-myristoyltransferase 1 (NMT1), mRNA (N-myristoyltransferase 1, isoform CRA_b)
MADESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKK
QKKKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFW
DTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENY
VEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEK
KMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRS
LNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQF
HLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAY
SFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYN
WKCPSMGAEKVGLVLQ
Enzyme 12 Number of Residues 496
Enzyme 12 Molecular Weight 56807
Enzyme 12 Theoretical pI 7.91
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function Not Available
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID A8K7C1 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name A8K7C1_HUMAN Link Image
Enzyme 12 PDB ID 1RXT Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AK291936 Link Image
Enzyme 12 GeneCard ID A8K7C1 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location 17
Enzyme 12 Locus 17q21.31
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 16712
Enzyme 13 Name cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name Not Available
Enzyme 13 Protein Sequence >cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEANEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
Enzyme 13 Number of Residues 397
Enzyme 13 Molecular Weight 41895.8
Enzyme 13 Theoretical pI 8.21
Enzyme 13 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 13 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 193786127 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID B3KNP8 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B3KNP8_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1194 bp
ATGGCTCTGCTCCGAGGTGTGTTTGTAGTTGCTGCTAAGCGAACGCCCTTTGGAGCTTAC
GGAGGCCTTCTGAAAGACTTCACTGCTACTGACTTGTCTGAATTTGCTGCCAAGGCTGCC
TTGTCTGCTGGCAAAGTCTCACCTGAAACAGTTGACAGTGTGATTATGGGCAATGTCCTG
CAGAGTTCTTCAGATGCTATATATTTGGCAAGGCATGTTGGTTTGCGTGTGGGAATCCCA
AAGGAGACCCCAGCTCTCACGATTAATAGGCTCTGTGGTTCTGGTTTTCAGTCCATTGTG
AATGGATGTCAGGAAATTTGTGTTAAAGAAGCTGAAGTTGTTTTATGTGGAGGAACCGAA
AGCATGAGCCAAGCTCCCTACTGTGTCAGAAATGTGCGTTTTGGAACCAAGCTTGGATCA
GATATCAAGCTGGAAGATTCTTTATGGGTATCATTAACAGATCAGCATGTCCAGCTCCCC
ATGGCAATGACTGCAGAGAATCTTGCTGTAAAACACAAAATAAGCAGAGAAGAATGTGAC
AAATATGCCCTGCAGTCACAGCAGAGATGGAAAGCTGCTAATGATGCTGGCTACTTTAAT
GATGAAATGGCACCAATTGAAGTGAAGACAAAGAAAGGAAAACAGACAATGCAGGTAGAC
GAGCATGCTCGGCCCCAAACCACCCTGGAACAGTTACAGAAACTTCCTCCAGTATTCAAG
AAAGATGGAACTGTTACTGCAGGGAATGCATCGGGTGTAGCTGATGGTGCTGGAGCTGTT
ATCATAGCTAGTGAAGATGCTGTTAAGAAACATAACTTCACACCACTGGCAAGAATTGTG
GGCTACTTTGTATCTGGATGTGATCCCTCTATCATGGGTATTGGTCCTGTCCCTGCTATC
AGTGGGGCACTGAAGAAAGCAGGACTGAGTCTTAAGGACATGGATTTGGTAGAGGCGAAT
GAAGCTTTTGCTCCCCAGTACTTGGCTGTTGAGAGGAGTTTGGATCTTGACATAAGTAAA
ACCAATGTGAATGGAGGAGCCATTGCTTTGGGTCACCCACTGGGAGGATCTGGATCAAGA
ATTACTGCACACCTGGTTCACGAATTAAGGCGTCGAGGTGGAAAATATGCCGTTGGATCA
GCTTGCATTGGAGGTGGCCAAGGTATTGCTGTCATCATTCAGAGCACAGCCTGA
Enzyme 13 GenBank Gene ID AK054673 Link Image
Enzyme 13 GeneCard ID Not Available
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID HGNC:83 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs Not Available
Enzyme 13 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 16766
Enzyme 14 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name NMT2
Enzyme 14 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPN
SGGTKSDSASDSQEIKIQQPSKNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQ
FWDTQPVPKLDEVITSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNE
NYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDS
VKKMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWH
RSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLK
QFHLAPVMDEEEVAHWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKA
AYSFYNIHTETPLLDLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYL
YNWRCPGTDSEKVGLVLQ
Enzyme 14 Number of Residues 498
Enzyme 14 Molecular Weight 56981
Enzyme 14 Theoretical pI 7.65
Enzyme 14 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID B0YJ49 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name B0YJ49_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID EF445001 Link Image
Enzyme 14 GeneCard ID B0YJ49 Link Image
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location 10
Enzyme 14 Locus 10p13
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 16884
Enzyme 15 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name NMT2
Enzyme 15 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase
KKRRSLPAEVLEGIWEPKRKRRNRREKRRNQIPEAPSQTRHLIPRRLKFSSLRNTTPSGS
RFQREQPWNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEVI
TSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDY
SPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHK
KLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKFS
HLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEVA
HWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLL
DLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVG
LVLQ
Enzyme 15 Number of Residues 484
Enzyme 15 Molecular Weight 56485
Enzyme 15 Theoretical pI 9.96
Enzyme 15 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID A8MWH3 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name A8MWH3_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID AL590365 Link Image
Enzyme 15 GeneCard ID A8MWH3 Link Image
Enzyme 15 GenAtlas ID NMT2 Link Image
Enzyme 15 HGNC ID HGNC:7858 Link Image
Enzyme 15 Chromosome Location 10
Enzyme 15 Locus 10p13
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 16885
Enzyme 16 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name NMT1
Enzyme 16 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase
DESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKKQK
KKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDT
QPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVE
DDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKM
VEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLN
PRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHL
TPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSF
YNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWK
CPSMGAEKVGLVLQ
Enzyme 16 Number of Residues 494
Enzyme 16 Molecular Weight 56603.6
Enzyme 16 Theoretical pI 7.91
Enzyme 16 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • N-terminal protein lipidation
  • N-terminal protein myristoylation
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
Enzyme 16 General Function Involved in glycylpeptide N-tetradecanoyltransferase activity
Enzyme 16 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide [RN:R03992]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 48257074 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q96HI4 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name Q96HI4_HUMAN Link Image
Enzyme 16 PDB ID 1RXT Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1485 bp
GACGAGAGTGAGACAGCAGTGAAGCCGCCGGCACCTCCGCTGCCGCAGATGATGGAAGGG
AACGGGAACGGCCATGAGCACTGCAGCGATTGCGAGAATGAGGAGGACAACAGCTACAAC
CGGGGTGGTTTGAGTCCAGCCAATGACACTGGAGCCAAAAAGAAGAAAAAGAAACAAAAA
AAGAAGAAAGAAAAAGGCAGTGAGACAGATTCAGCCCAGGATCAGCCTGTGAAGATGAAC
TCTTTGCCAGCAGAGAGGATCCAGGAAATACAGAAGGCCATTGAGCTGTTCTCAGTGGGT
CAGGGACCTGCCAAAACCATGGAGGAGGCTAGCAAGCGAAGCTACCAGTTCTGGGATACG
CAGCCCGTCCCCAAGCTGGGCGAAGTGGTGAACACCCATGGCCCCGTGGAGCCTGACAAG
GACAATATCCGCCAGGAGCCCTACACCCTGCCCCAGGGCTTCACCTGGGATGCTTTGGAC
CTGGGCGATCGTGGTGTGCTAAAAGAACTGTACACCCTCCTGAATGAGAACTATGTGGAA
GATGATGACAACATGTTCCGATTTGATTATTCCCCGGAGTTTCTTTTGTGGGCTCTCCGG
CCACCCGGCTGGCTCCCCCAGTGGCACTGTGGGGTTCGAGTGGTCTCAAGTCGGAAATTG
GTTGGGTTCATTAGCGCCATCCCAGCAAACATCCATATCTATGACACAGAGAAGAAGATG
GTAGAGATCAACTTCCTGTGTGTCCACAAGAAGCTGCGTTCCAAGAGGGTTGCTCCAGTT
CTGATCCGAGAGATCACCAGGCGGGTTCACCTGGAGGGCATCTTCCAAGCAGTTTACACT
GCCGGGGTGGTACTACCAAAGCCTGTTGGCACCTGCAGGTATTGGCATCGGTCCCTAAAC
CCACGGAAGCTGATTGAAGTGAAGTTCTCCCACCTGAGCAGAAATATGACCATGCAGCGC
ACCATGAAGCTCTACCGACTGCCAGAGACTCCCAAGACAGCTGGGCTGCGACCAATGGAA
ACAAAGGACATTCCAGTAGTGCACCAGCTCCTCACCAGGTACTTGAAGCAATTTCACCTT
ACGCCCGTCATGAGCCAGGAGGAGGTGGAGCACTGGTTCTACCCCCAGGAGAATATCATC
GACACTTTCGTGGTGGAGAACGCAAACGGAGAGGTGACAGATTTCCTGAGCTTTTATACG
CTGCCCTCCACCATCATGAACCATCCAACCCACAAGAGTCTCAAAGCTGCTTATTCTTTC
TACAACGTTCACACCCAGACCCCTCTTCTAGACCTCATGAGCGACGCCCTTGTCCTCGCC
AAAATGAAAGGGTTTGATGTGTTCAATGCACTGGATCTCATGGAGAACAAAACCTTCCTG
GAGAAGCTCAAGTTTGGCATAGGGGACGGCAACCTGCAGTATTACCTTTACAATTGGAAA
TGCCCCAGCATGGGGGCAGAGAAGGTTGGACTGGTGCTACAATAA
Enzyme 16 GenBank Gene ID BC008579 Link Image
Enzyme 16 GeneCard ID NMT1 Link Image
Enzyme 16 GenAtlas ID NMT1 Link Image
Enzyme 16 HGNC ID HGNC:7857 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 17q21.31
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 16886
Enzyme 17 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name NMT2
Enzyme 17 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPN
SGGTKSDSASDSQEIKIQQPSKHNTIWQQISAGAAMGSATMEGEWTGMRNDHRNPSVPMQ
KLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEVITSHGAIEPDKDNVRQ
EPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWL
LQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHKKLRSKRVAPVLIREI
TRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLY
RLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEVAHWFLPREHIIDTFVV
ESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMSDALILAKSKGF
DVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVRLVLN
Enzyme 17 Number of Residues 529
Enzyme 17 Molecular Weight 60491.6
Enzyme 17 Theoretical pI 7.68
Enzyme 17 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • N-terminal protein lipidation
  • N-terminal protein myristoylation
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
Enzyme 17 General Function Involved in glycylpeptide N-tetradecanoyltransferase activity
Enzyme 17 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide [RN:R03992]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 55665859 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID A8MWF5 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name A8MWF5_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1590 bp
ATGGCGGAGGACAGCGAGTCTGCGGCCAGCCAGCAGAGCCTGGAACTGGACGACCAGGAC
ACGTGCGGGATAGACGGGGACAATGAGGAGGAGACGGAGCACGCCAAAGGAAGTCCTGGA
GGGTATTTGGGAGCCAAAAAGAAAAAGAAGAAACAGAAGAGAAAAAAGGAGAAACCAAAT
TCCGGAGGCACCAAGTCAGACTCGGCATCTGATTCCCAGGAGATTAAAATTCAGCAGCCT
TCGAAACACAACACCATCTGGCAGCAGATTTCAGCGGGAGCAGCCATGGGTAGTGCTACT
ATGGAAGGTGAATGGACAGGCATGAGAAATGATCATAAGAATCCCAGTGTTCCAATGCAG
AAGTTGCAGGATATCCAGAGAGCAATGGAGCTGCTATCCGCATGCCAGGGCCCAGCCAGG
AACATTGATGAGGCTGCAAAGCACAGATACCAGTTTTGGGACACACAACCGGTACCAAAA
CTAGATGAAGTCATAACATCTCATGGTGCAATTGAACCAGATAAAGACAACGTACGCCAA
GAACCGTATTCTTTGCCACAGGGTTTTATGTGGGACACTTTAGACTTGAGTGATGCCGAA
GTGCTCAAGGAGTTATACACGTTGTTAAATGAGAATTACGTAGAAGATGATGACAATATG
TTCCGATTTGACTATTCACCCGAGTTCCTGTTGTGGGCTCTGCGTCCACCAGGCTGGCTC
CTGCAGTGGCACTGTGGGGTCAGAGTGTCTTCAAATAAAAAACTGGTCGGGTTCATAAGT
GCCATCCCAGCAAACATTCGGATTTATGACAGTGTGAAGAAGATGGTAGAAATCAACTTT
CTTTGTGTTCATAAGAAGTTGAGATCGAAACGGGTAGCCCCAGTGCTAATCCGAGAGATC
ACTAGAAGAGTGAACCTGGAAGGGATCTTCCAGGCTGTGTACACCGCGGGAGTGGTTCTT
CCTAAGCCCATAGCCACATGCAGATACTGGCATCGATCACTAAACCCCAGAAAATTGGTA
GAAGTGAAATTTTCTCACTTGAGTAGAAATATGACTTTACAGAGAACAATGAAGCTATAC
AGACTTCCAGATGTTACAAAGACTTCAGGTTTGAGACCAATGGAACCAAAAGATATCAAA
TCAGTTCGAGAATTAATCAACACTTACCTGAAGCAGTTTCATCTGGCTCCAGTGATGGAT
GAAGAGGAAGTAGCCCACTGGTTCCTCCCCCGGGAGCACATTATTGACACGTTTGTAGTG
GAGAGCCCCAACGGTAAACTGACTGATTTCCTGAGCTTCTATACGCTCCCCTCCACGGTG
ATGCACCACCCTGCTCACAAGAGCCTCAAAGCCGCCTACTCATTCTACAACATCCACACA
GAGACGCCCCTGCTGGACCTCATGAGCGACGCGCTCATCCTGGCTAAATCGAAAGGATTT
GATGTATTCAATGCACTGGATTTGATGGAAAATAAGACATTCTTGGAAAAACTCAAGTTT
GGTATAGGAGATGGCAATTTGCAGTATTACCTGTACAATTGGAGGTGTCCAGGTACAGAT
TCTGAAAAGGTTGGACTAGTACTACAATAG
Enzyme 17 GenBank Gene ID AL590365 Link Image
Enzyme 17 GeneCard ID NMT2 Link Image
Enzyme 17 GenAtlas ID NMT2 Link Image
Enzyme 17 HGNC ID HGNC:7858 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 10p13
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 16887
Enzyme 18 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name NMT2
Enzyme 18 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPN
SGGTKSDSASDSQEIKIQQPSKHNTIWQQISAGAAMGSATMEGEWTGMRNDHKNPSVPMQ
KLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEVITSHGAIEPDKDNVRQ
EPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWL
LQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHKKLRSKRVAPVLIREI
TRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLY
RLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEVAHWFLPREHIIDTFVV
ESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMSDALILAKSKGF
DVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVGLVLQ
Enzyme 18 Number of Residues 529
Enzyme 18 Molecular Weight 60378.5
Enzyme 18 Theoretical pI 7.46
Enzyme 18 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • N-terminal protein lipidation
  • N-terminal protein myristoylation
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
Enzyme 18 General Function Involved in glycylpeptide N-tetradecanoyltransferase activity
Enzyme 18 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions
  • tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide [RN:R03992]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 55665859 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q5VUC7 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name Q5VUC7_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1590 bp
ATGGCGGAGGACAGCGAGTCTGCGGCCAGCCAGCAGAGCCTGGAACTGGACGACCAGGAC
ACGTGCGGGATAGACGGGGACAATGAGGAGGAGACGGAGCACGCCAAAGGAAGTCCTGGA
GGGTATTTGGGAGCCAAAAAGAAAAAGAAGAAACAGAAGAGAAAAAAGGAGAAACCAAAT
TCCGGAGGCACCAAGTCAGACTCGGCATCTGATTCCCAGGAGATTAAAATTCAGCAGCCT
TCGAAACACAACACCATCTGGCAGCAGATTTCAGCGGGAGCAGCCATGGGTAGTGCTACT
ATGGAAGGTGAATGGACAGGCATGAGAAATGATCATAAGAATCCCAGTGTTCCAATGCAG
AAGTTGCAGGATATCCAGAGAGCAATGGAGCTGCTATCCGCATGCCAGGGCCCAGCCAGG
AACATTGATGAGGCTGCAAAGCACAGATACCAGTTTTGGGACACACAACCGGTACCAAAA
CTAGATGAAGTCATAACATCTCATGGTGCAATTGAACCAGATAAAGACAACGTACGCCAA
GAACCGTATTCTTTGCCACAGGGTTTTATGTGGGACACTTTAGACTTGAGTGATGCCGAA
GTGCTCAAGGAGTTATACACGTTGTTAAATGAGAATTACGTAGAAGATGATGACAATATG
TTCCGATTTGACTATTCACCCGAGTTCCTGTTGTGGGCTCTGCGTCCACCAGGCTGGCTC
CTGCAGTGGCACTGTGGGGTCAGAGTGTCTTCAAATAAAAAACTGGTCGGGTTCATAAGT
GCCATCCCAGCAAACATTCGGATTTATGACAGTGTGAAGAAGATGGTAGAAATCAACTTT
CTTTGTGTTCATAAGAAGTTGAGATCGAAACGGGTAGCCCCAGTGCTAATCCGAGAGATC
ACTAGAAGAGTGAACCTGGAAGGGATCTTCCAGGCTGTGTACACCGCGGGAGTGGTTCTT
CCTAAGCCCATAGCCACATGCAGATACTGGCATCGATCACTAAACCCCAGAAAATTGGTA
GAAGTGAAATTTTCTCACTTGAGTAGAAATATGACTTTACAGAGAACAATGAAGCTATAC
AGACTTCCAGATGTTACAAAGACTTCAGGTTTGAGACCAATGGAACCAAAAGATATCAAA
TCAGTTCGAGAATTAATCAACACTTACCTGAAGCAGTTTCATCTGGCTCCAGTGATGGAT
GAAGAGGAAGTAGCCCACTGGTTCCTCCCCCGGGAGCACATTATTGACACGTTTGTAGTG
GAGAGCCCCAACGGTAAACTGACTGATTTCCTGAGCTTCTATACGCTCCCCTCCACGGTG
ATGCACCACCCTGCTCACAAGAGCCTCAAAGCCGCCTACTCATTCTACAACATCCACACA
GAGACGCCCCTGCTGGACCTCATGAGCGACGCGCTCATCCTGGCTAAATCGAAAGGATTT
GATGTATTCAATGCACTGGATTTGATGGAAAATAAGACATTCTTGGAAAAACTCAAGTTT
GGTATAGGAGATGGCAATTTGCAGTATTACCTGTACAATTGGAGGTGTCCAGGTACAGAT
TCTGAAAAGGTTGGACTAGTACTACAATAG
Enzyme 18 GenBank Gene ID AL590365 Link Image
Enzyme 18 GeneCard ID NMT2 Link Image
Enzyme 18 GenAtlas ID NMT2 Link Image
Enzyme 18 HGNC ID HGNC:7858 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 10p13
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 16888
Enzyme 19 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name NMT2
Enzyme 19 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase
MRRRRSTPKEVLEGIWEPKRKRRNRREKRRNQIPEAPSQTRHLIPRRLKFSSLRNTTPSG
SRFQREQPWNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEV
ITSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFD
YSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVH
KKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKF
SHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEV
AHWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPL
LDLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKV
GLVLQ
Enzyme 19 Number of Residues 485
Enzyme 19 Molecular Weight 56716.1
Enzyme 19 Theoretical pI 10.02
Enzyme 19 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • N-terminal protein lipidation
  • N-terminal protein myristoylation
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
Enzyme 19 General Function Involved in glycylpeptide N-tetradecanoyltransferase activity
Enzyme 19 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions
  • tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide [RN:R03992]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 55665860 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q5VUC6 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name Q5VUC6_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1458 bp
ATGAGGAGGAGACGGAGCACGCCAAAGGAAGTCCTGGAGGGTATTTGGGAGCCAAAAAGA
AAAAGAAGAAACAGAAGAGAAAAAAGGAGAAACCAAATTCCGGAGGCACCAAGTCAGACT
CGGCATCTGATTCCCAGGAGATTAAAATTCAGCAGCCTTCGAAACACAACACCATCTGGC
AGCAGATTTCAGCGGGAGCAGCCATGGAATCCCAGTGTTCCAATGCAGAAGTTGCAGGAT
ATCCAGAGAGCAATGGAGCTGCTATCCGCATGCCAGGGCCCAGCCAGGAACATTGATGAG
GCTGCAAAGCACAGATACCAGTTTTGGGACACACAACCGGTACCAAAACTAGATGAAGTC
ATAACATCTCATGGTGCAATTGAACCAGATAAAGACAACGTACGCCAAGAACCGTATTCT
TTGCCACAGGGTTTTATGTGGGACACTTTAGACTTGAGTGATGCCGAAGTGCTCAAGGAG
TTATACACGTTGTTAAATGAGAATTACGTAGAAGATGATGACAATATGTTCCGATTTGAC
TATTCACCCGAGTTCCTGTTGTGGGCTCTGCGTCCACCAGGCTGGCTCCTGCAGTGGCAC
TGTGGGGTCAGAGTGTCTTCAAATAAAAAACTGGTCGGGTTCATAAGTGCCATCCCAGCA
AACATTCGGATTTATGACAGTGTGAAGAAGATGGTAGAAATCAACTTTCTTTGTGTTCAT
AAGAAGTTGAGATCGAAACGGGTAGCCCCAGTGCTAATCCGAGAGATCACTAGAAGAGTG
AACCTGGAAGGGATCTTCCAGGCTGTGTACACCGCGGGAGTGGTTCTTCCTAAGCCCATA
GCCACATGCAGATACTGGCATCGATCACTAAACCCCAGAAAATTGGTAGAAGTGAAATTT
TCTCACTTGAGTAGAAATATGACTTTACAGAGAACAATGAAGCTATACAGACTTCCAGAT
GTTACAAAGACTTCAGGTTTGAGACCAATGGAACCAAAAGATATCAAATCAGTTCGAGAA
TTAATCAACACTTACCTGAAGCAGTTTCATCTGGCTCCAGTGATGGATGAAGAGGAAGTA
GCCCACTGGTTCCTCCCCCGGGAGCACATTATTGACACGTTTGTAGTGGAGAGCCCCAAC
GGTAAACTGACTGATTTCCTGAGCTTCTATACGCTCCCCTCCACGGTGATGCACCACCCT
GCTCACAAGAGCCTCAAAGCCGCCTACTCATTCTACAACATCCACACAGAGACGCCCCTG
CTGGACCTCATGAGCGACGCGCTCATCCTGGCTAAATCGAAAGGATTTGATGTATTCAAT
GCACTGGATTTGATGGAAAATAAGACATTCTTGGAAAAACTCAAGTTTGGTATAGGAGAT
GGCAATTTGCAGTATTACCTGTACAATTGGAGGTGTCCAGGTACAGATTCTGAAAAGGTT
GGACTAGTACTACAATAG
Enzyme 19 GenBank Gene ID AL590365 Link Image
Enzyme 19 GeneCard ID NMT2 Link Image
Enzyme 19 GenAtlas ID NMT2 Link Image
Enzyme 19 HGNC ID HGNC:7858 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 10p13
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 16889
Enzyme 20 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 20 Synonyms Not Available
Enzyme 20 Gene Name NMT1
Enzyme 20 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase
YWAGLRPMETKDIPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIIDTFVVENANGE
VTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQTPLLDLMSDALVLAKMVRSRRGGLW
RCAGKGQWSHGEHSSRDAASHGLEALSPPHLFCLGRVPAVFRQKLKTWREQGASEVKALN
SS
Enzyme 20 Number of Residues 182
Enzyme 20 Molecular Weight 20763.6
Enzyme 20 Theoretical pI 8.69
Enzyme 20 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • N-terminal protein lipidation
  • N-terminal protein myristoylation
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
Enzyme 20 General Function Involved in glycylpeptide N-tetradecanoyltransferase activity
Enzyme 20 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions
  • tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide [RN:R03992]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 133777378 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID A4FU65 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name A4FU65_HUMAN Link Image
Enzyme 20 PDB ID 1RXT Link Image
Enzyme 20 PDB File Show
Enzyme 20 3D Structure
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >551 bp
GCTACTGGGCTGGGCTGCGACCAATGGAAACAAAGGACATTCCAGTAGTGCACCAGCTCC
TCACCAGGTACTTGAAGCAATTTCACCTTACGCCCGTCATGAGCCAGGAGGAGGTGGAGC
ACTGGTTCTACCCCCAGGAGAATATCATCGACACTTTCGTGGTGGAGAACGCAAACGGAG
AGGTGACAGATTTCCTGAGCTTTTATACGCTGCCCTCCACCATCATGAACCATCCAACCC
ACAAGAGTCTCAAAGCTGCTTATTCTTTCTACAACGTTCACACCCAGACCCCTCTTCTAG
ACCTCATGAGCGACGCCCTTGTCCTCGCCAAAATGGTGAGGAGCAGACGGGGGGGTCTCT
GGAGATGTGCAGGGAAGGGGCAGTGGAGCCATGGTGAGCACAGCTCCCGGGACGCGGCCT
CCCATGGGCTGGAGGCTCTGAGCCCTCCTCATCTGTTCTGCTTAGGCAGGGTTCCCGCAG
TTTTTAGGCAGAAACTCAAAACTTGGAGGGAACAAGGAGCATCCGAAGTGAAGGCATTGA
ACTCCTCCTGA
Enzyme 20 GenBank Gene ID BC109226 Link Image
Enzyme 20 GeneCard ID NMT1 Link Image
Enzyme 20 GenAtlas ID Not Available
Enzyme 20 HGNC ID Not Available
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 17q21.31
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available