|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5270 |
| Enzyme 1 Name |
Pyruvate dehydrogenase protein X component, mitochondrial |
| Enzyme 1 Synonyms |
- Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
- E3-binding protein
- E3BP
- Lipoyl-containing pyruvate dehydrogenase complex component X
- proX
|
| Enzyme 1 Gene Name |
PDHX |
| Enzyme 1 Protein Sequence |
>Pyruvate dehydrogenase protein X component, mitochondrial
MAASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLRGDPIKIL
MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK
NIRLGSLIGLIVEEGEDWKHVEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTL
RFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKITESRPTPAPTAT
PTAPSPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPH
AYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPF
IDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNL
GMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEEGNAKLQQRQLITVTMSSDSRVVDD
ELATRFLKSFKANLENPIRLA
|
| Enzyme 1 Number of Residues |
501 |
| Enzyme 1 Molecular Weight |
54121.8 |
| Enzyme 1 Theoretical pI |
9.09 |
| Enzyme 1 GO Classification |
| Function |
- acyltransferase activity
- binding
- catalytic activity
- protein binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in acyltransferase activity |
| Enzyme 1 Specific Function |
Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex |
| Enzyme 1 Pathways |
Not Available |
| Enzyme 1 Reactions |
Not Available |
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
2316040  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O00330  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ODPX_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1506 bp
ATGGCGGCCTCCTGGAGGCTGGGCTGTGATCCGCGGCTGCTGCGTTATCTTGTGGGCTTC
CCTGGCTGCCGAAGCGTAGGGCTGGTGAAGGGGGCTCTTGGGTGGTCCGTAAGCCGCGGA
GCTAATTGGAGATGGTTTCACAGCACGCAGTGGCTTCGGGGTGATCCCATTAAGATACTA
ATGCCATCACTGTCTCCTACAATGGAAGAAGGAAACATTGTGAAATGGCTGAAAAAGGAA
GGTGAAGCGGTGAGTGCTGGAGATGCATTATGTGAAATTGAGACTGACAAAGCTGTGGTT
ACCTTAGATGCAAGTGATGATGGAATCTTGGCCAAAATCGTGGTTGAAGAAGGAAGTAAA
AATATACGGCTAGGTTCACTAATTGGTTTGATAGTAGAAGAAGGAGAAGATTGGAAACAT
GTTGAAATTCCCAAAGACGTAGGTCCTCCACCACCAGTTTCAAAACCTTCAGAGCCTCGC
CCCTCACCAGAACCACAGATTTCCATCCCTGTCAAGAAGGAACACATACCCGGGACACTA
CGGTTCCGTTTAAGTCCAGCTGCCCGCAATATTCTGGAAAAACACTCACTGGATGCTAGC
CAGGGCACAGCCACTGGCCCTCGGGGGATATTCACTAAAGAGGATGCTCTCAAACTTGTC
CAGTTGAAACAAACGGGCAAGATTACCGAGTCCAGACCAACTCCAGCCCCCACAGCCACT
CCCACAGCACCTTCGCCCCTACAGGCCACATCTGGACCATCTTATCCCCGGCCTGTGATC
CCACCAGTATCAACTCCCGGACAACCCAATGCAGTGGGCACATTCACTGAAATCCCCGCC
AGCAATATTCGAAGAGTTATTGCCAAGAGATTAACTGAATCTAAAAGTACTGTACCTCAT
GCATATGCTACTGCTGACTGTGACCTTGGAGCTGTTTTAAAAGTTAGGCAAGATCTGGTC
AAAGATGACATTAAAGTATCAGTAAATGATTTTATCATCAAGGCAGCAGCTGTTACCCTT
AAACAAATGCCAGATGTTAATGTAAGCTGGGATGGAGAGGGCCCAAAGCAACTGCCATTT
ATTGACATTTCAGTGGCTGTGGCAACAGATAAAGGCTTACTTACTCCAATCATAAAAGAT
GCTGCTGCTAAAGGTATCCAGGAAATTGCTGACTCTGTAAAGGCTCTATCAAAGAAAGCA
AGAGATGGAAAATTGTTGCCTGAAGAATACCAAGGAGGATCTTTTAGTATTTCCAACTTG
GGGATGTTTGGCATCGACGAATTTACTGCAGTGATTAACCCTCCTCAGGCCTGCATTTTG
GCGGTTGGGAGGTTCCGACCTGTGCTGAAGCTCACTGAGGATGAAGAGGGAAATGCCAAA
CTGCAGCAGCGCCAGCTCATAACAGTCACAATGTCAAGTGACAGTCGAGTGGTTGATGAC
GAACTGGCAACCAGGTTTCTTAAAAGTTTTAAAGCAAACCTAGAGAATCCTATCCGACTT
GCCTAG
|
| Enzyme 1 GenBank Gene ID |
AF001437  |
| Enzyme 1 GeneCard ID |
PDHX  |
| Enzyme 1 GenAtlas ID |
PDHX  |
| Enzyme 1 HGNC ID |
HGNC:21350  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
11p13 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Harris RA, Bowker-Kinley MM, Wu P, Jeng J, Popov KM: Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex. J Biol Chem. 1997 Aug 8;272(32):19746-51. [PubMed
]
- Aral B, Benelli C, Ait-Ghezala G, Amessou M, Fouque F, Maunoury C, Creau N, Kamoun P, Marsac C: Mutations in PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase-complex gene on chromosome 11p1, in congenital lactic acidosis. Am J Hum Genet. 1997 Dec;61(6):1318-26. [PubMed
]
- Ling M, McEachern G, Seyda A, MacKay N, Scherer SW, Bratinova S, Beatty B, Giovannucci-Uzielli ML, Robinson BH: Detection of a homozygous four base pair deletion in the protein X gene in a case of pyruvate dehydrogenase complex deficiency. Hum Mol Genet. 1998 Mar;7(3):501-5. [PubMed
]
- 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
]
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed
]
- 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
]
- Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS: How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex. J Biol Chem. 2006 Jan 6;281(1):648-55. Epub 2005 Nov 1. [PubMed
]
- Brautigam CA, Wynn RM, Chuang JL, Machius M, Tomchick DR, Chuang DT: Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex. Structure. 2006 Mar;14(3):611-21. Epub 2006 Jan 26. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5284 |
| Enzyme 2 Name |
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial |
| Enzyme 2 Synonyms |
- 70 kDa mitochondrial autoantigen of primary biliary cirrhosis
- PBC
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- M2 antigen complex 70 kDa subunit
- Pyruvate dehydrogenase complex component E2
- PDC-E2
- PDCE2
|
| Enzyme 2 Gene Name |
DLAT |
| Enzyme 2 Protein Sequence |
>Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
MWRVCARRAQNVAPWAGLEARWTALQEVPGTPRVTSRSGPAPARRNSVTTGYGGVRALCG
WTPSSGATPRNRLLLQLLGSPGRRYYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGDKIN
EGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAFKNYT
LDSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPHMQVLLPALSPTMTMGTVQRWEK
KVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI
SAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPL
AKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVF
TDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFI
IKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIAND
VVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPA
DNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL
|
| Enzyme 2 Number of Residues |
647 |
| Enzyme 2 Molecular Weight |
68996.0 |
| Enzyme 2 Theoretical pI |
7.94 |
| Enzyme 2 GO Classification |
| Function |
- S-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- dihydrolipoyllysine-residue acetyltransferase activity
- protein binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
- pyruvate metabolic process
|
| Component |
- macromolecular complex
- protein complex
- pyruvate dehydrogenase complex
|
|
| Enzyme 2 General Function |
Involved in acyltransferase activity |
| Enzyme 2 Specific Function |
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine [RN:R02569]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
62898924  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P10515  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ODP2_HUMAN  |
| Enzyme 2 PDB ID |
1FYC  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1944 bp
ATGTGGCGCGTCTGTGCGCGACGGGCTCAGAATGTAGCCCCATGGGCGGGACTCGAGGCT
CGGTGGACGGCCTTGCAGGAGGTACCCGGAACTCCACGAGTGACCTCGCGATCTGGCCCG
GCTCCCGTTCGTCGCAACAGCGTGACTACAGGGTATGGCGGGGTCCGGGCACTGTGCGGC
TGGACCCCCAGTTCTGGGGCCACGCCGCGGAACCGCTTACTGCTGCAGCTTTTGGGGTCG
CCCGGCCGCCGCTATTACAGTCTTCCCCCGCATCAGAAGGTTCCATTGCCTTCTCTTTCC
CCCACAATGCAGGCAGGCACCATAGCCCGTTGGGAAAAAAAAGAGGGAGACAAAATCAAT
GAAGGTGACCTAATTGCAGAGGTTGAAACTGATAAAGCCACTGTTGGATTTGAGAGCCTG
GAGGAGTGTTATATGGCAAAGATACTTGTTGCTGAAGGTACCAGGGATGTTCCCATCGGA
GCGATCATCTGTATCACAGTTGGCAAGCCTGAGGATATTGAGGCCTTTAAAAATTATACA
CTGGATTCCTCAGCAGCACCTACCCCACAAGCGGCCCCAGCACCAACCCCTGCTGCCACT
GCTTCGCCACCTACACCTTCTGCTCAGGCTCCTGGTAGCTCATATCCCCCTCACATGCAG
GTACTTCTTCCTGCCCTCTCTCCCACCATGACCATGGGCACAGTTCAGAGATGGGAAAAA
AAAGTGGGTGAGAAGCTAAGTGAAGGAGACTTACTGGCAGAGATAGAAACTGACAAAGCC
ACTATAGGTTTTGAAGTACAGGAAGAAGGTTATCTGGCAAAAATCCTGGTCCCTGAAGGC
ACAAGAGATGTCCCTCTAGGAACCCCACTCTGTATCATTGTAGAAAAAGAGGCAGATATA
TCAGCATTTGCTGACTATAGGCCAACCGAAGTAACAGATTTAAAACCACAAGCGCCACCA
CCTACCCCACCCCCGGTGGCCGCTGTTCCTCCAACTCCCCAGCCTTTAGCTCCTACACCT
TCAGCACCCTGCCCAGCTACTCCTGCTGGACCAAAGGGAAGGGTGTTTGTTAGCCCTCTT
GCAAAGAAGTTGGCAGTAGAGAAAGGGATTGATCTTACACAAGTAAAAGGGACAGGACCA
GATGGTAGAATCACCAAGAAGGATATCGACTCTTTTGTGCCTAGTAAAGTTGCTCCTGCT
CCGGCAGCTGTTGTGCCTCCCACAGGTCCTGGAATGGCACCAGTTCCTACAGGTGTCTTC
ACAGATATCCCAATCAGCAACATTCGTCGGGTTATTGCACAGCGATTAATGCAATCAAAG
CAAACCATACCTCATTATTACCTTTCTATCAATGTAAATATGGGAGAAGTTTTGTTGGTA
CGGAAAGAACTTAATAAGATATTAGAAGGGAGAAGCAAAATTTCTGTCAATGACTTCATC
ATAAAAGCTTCAGCTTTGGCATGTTTAAAAGTTCCCGAAGCAAATTCTTCTTGGATGGAC
ACAGTTATAAGACAAAATCATGTTGTTGATGTCAGTGTTGCGGTCAGTACTCCTGCAGGA
CTCATCACACCTATTGTGTTTAATGCACATATAAAAGGAGTGGAAACCATTGCTAATGAT
GTTGTTTCTTTAGCAACCAAAGCAAGAGAGGGTAAACTACAGCCACATGAATTCCAGGGT
GGCACTTTTACGATCTCCAATTTAGGAATGTTTGGAATTAAGAATTTCTCTGCTATTATT
AACCCACCTCAAGCATGTATTTTGGCAATTGGTGCTTCAGAGGATAAACTGGTCCCTGCA
GATAATGAAAAAGGGTTTGATGTGGCTAGCATGATGTCTGTTACACTCAGTTGTGATCAC
CGGGTGGTGGATGGAGCAGTTGGAGCCCAGTGGCTTGCTGAGTTTAGAAAGTACCTTGAA
AAACCTATCACTATGTTGTTGTAA
|
| Enzyme 2 GenBank Gene ID |
AK223596  |
| Enzyme 2 GeneCard ID |
DLAT  |
| Enzyme 2 GenAtlas ID |
DLAT  |
| Enzyme 2 HGNC ID |
HGNC:2896  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
11q23.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed
]
- Coppel RL, McNeilage LJ, Surh CD, Van de Water J, Spithill TW, Whittingham S, Gershwin ME: Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7317-21. [PubMed
]
- Thekkumkara TJ, Ho L, Wexler ID, Pons G, Liu TC, Patel MS: Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex. FEBS Lett. 1988 Nov 21;240(1-2):45-8. [PubMed
]
- 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
]
- Howard MJ, Fuller C, Broadhurst RW, Perham RN, Tang JG, Quinn J, Diamond AG, Yeaman SJ: Three-dimensional structure of the major autoantigen in primary biliary cirrhosis. Gastroenterology. 1998 Jul;115(1):139-46. [PubMed
]
- Head RA, Brown RM, Zolkipli Z, Shahdadpuri R, King MD, Clayton PT, Brown GK: Clinical and genetic spectrum of pyruvate dehydrogenase deficiency: dihydrolipoamide acetyltransferase (E2) deficiency. Ann Neurol. 2005 Aug;58(2):234-41. [PubMed
]
- Kato M, Chuang JL, Tso SC, Wynn RM, Chuang DT: Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex. EMBO J. 2005 May 18;24(10):1763-74. Epub 2005 Apr 28. [PubMed
]
- Devedjiev Y, Steussy CN, Vassylyev DG: Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications. J Mol Biol. 2007 Jul 13;370(3):407-16. Epub 2007 May 10. [PubMed
]
- Kato M, Li J, Chuang JL, Chuang DT: Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol. Structure. 2007 Aug;15(8):992-1004. Epub 2007 Aug 2. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5415 |
| Enzyme 3 Name |
NADPH--cytochrome P450 reductase |
| Enzyme 3 Synonyms |
- CPR
- P450R
|
| Enzyme 3 Gene Name |
POR |
| Enzyme 3 Protein Sequence |
>NADPH--cytochrome P450 reductase
MGDSHVDTSSTVSEAVAEEVSLFSMTDMILFSLIVGLLTYWFLFRKKKEEVPEFTKIQTL
TSSVRESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLA
DLSSLPEIDNALVVFCMATYGEGDPTDNAQDFYDWLQETDVDLSGVKFAVFGLGNKTYEH
FNAMGKYVDKRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEHFGVEATGEES
SIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHL
MHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHP
FPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWV
VEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYET
KAGRINKGVATNWLRAKEPAGENGGRALVPMFVRKSQFRLPFKATTPVIMVGPGTGVAPF
IGFIQERAWLRQQGKEVGETLLYYGCRRSDEDYLYREELAQFHRDGALTQLNVAFSREQS
HKVYVQHLLKQDREHLWKLIEGGAHIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVD
YIKKLMTKGRYSLDVWS
|
| Enzyme 3 Number of Residues |
677 |
| Enzyme 3 Molecular Weight |
76689.1 |
| Enzyme 3 Theoretical pI |
5.28 |
| Enzyme 3 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- nucleotide binding
- oxidoreductase activity
- transition metal ion binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in oxidoreductase activity |
| Enzyme 3 Specific Function |
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5 |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
11414998  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P16435  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NCPR_HUMAN  |
| Enzyme 3 PDB ID |
1AMO  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2034 bp
ATGGGAGACTCCCACGTGGACACCAGCTCCACCGTGTCCGAGGCGGTGGCCGAAGAAGTA
TCTCTTTTCAGCATGACGGACATGATTCTGTTTTCGCTCATCGTGGGTCTCCTAACCTAC
TGGTTCCTCTTCAGAAAGAAAAAAGAAGAAGTCCCCGAGTTCACCAAAATTCAGACATTG
ACCTCCTCTGTCAGAGAGAGCAGCTTTGTGGAAAAGATGAAGAAAACGGGGAGGAACATC
ATCGTGTTCTACGGCTCCCAGACGGGGACTGCAGAGGAGTTTGCCAACCGCCTGTCCAAG
GACGCCCACCGCTACGGGATGCGAGGCATGTCAGCGGACCCTGAGGAGTATGACCTGGCC
GACCTGAGCAGCCTGCCAGAGATCGACAACGCCCTGGTGGTTTTCTGCATGGCCACCTAC
GGTGAGGGAGACCCCACCGACAATGCCCAGGACTTCTACGACTGGCTGCAGGAGACAGAC
GTGGATCTCTCTGGGGTCAAGTTCGCGGTGTTTGGTCTTGGGAACAAGACCTACGAGCAC
TTCAATGCCATGGGCAAGTACGTGGACAAGCGGCTGGAGCAGCTCGGCGCCCAGCGCATC
TTTGAGCTGGGGTTGGGCGACGACGATGGGAACTTGGAGGAGGACTTCATCACCTGGCGA
GAGCAGTTCTGGCCGGCCGTGTGTGAACACTTTGGGGTGGAAGCCACTGGCGAGGAGTCC
AGCATTCGCCAGTACGAGCTTGTGGTCCACACCGACATAGATGCGGCCAAGGTGTACATG
GGGGAGATGGGCCGGCTGAAGAGCTACGAGAACCAGAAGCCCCCCTTTGATGCCAAGAAT
CCGTTCCTGGCTGCAGTCACCACCAACCGGAAGCTGAACCAGGGAACCGAGCGCCACCTC
ATGCACCTGGAATTGGACATCTCGGACTCCAAAATCAGGTATGAATCTGGGGACCACGTG
GCTGTGTACCCAGCCAACGACTCTGCTCTCGTCAACCAGCTGGGCAAAATCCTGGGTGCC
GACCTGGACGTCGTCATGTCCCTGAACAACCTGGATGAGGAGTCCAACAAGAAGCACCCA
TTCCCGTGCCCTACGTCCTACCGCACGGCCCTCACCTACTACCTGGACATCACCAACCCG
CCGCGTACCAACGTGCTGTACGAGCTGGCGCAGTACGCCTCGGAGCCCTCGGAGCAGGAG
CTGCTGCGCAAGCTGGCCTCCTCCTCCGGCGAGGGCAAGGAGCTGTACCTGAGCTGGGTG
GTGGAGGCCCGGAGGCACATCCTGGCCATCCTGCAGGACTGCCCGTCCCTGCGGCCCCCC
ATCGACCACCTGTGTGAGCTGCTGCCGCGCCTGCAGGCCCGCTACTACTCCATCGCCTCA
TCCTCCAAGGTCCACCCCAACTCTGTGCACATCTGTGCGGTGGTTGTGGAGTACGAGACC
AAGGCCGGCCGCATCAACAAGGGCGTGGCCACCAACTGGCTGCGGGCCAAGGAGCCTGCC
GGGGAGAACGGCGGCCGTGCGCTGGTGCCCATGTTCGTGCGCAAGTCCCAGTTACGCCTG
CCCTTCAAGGCCACCACGCCTGTCATCATGGTGGGCCCCGGCACCGGGGTGGCACCCTTC
ATAGGCTTCATCCAGGAGCGGGCCTGGCTGCGACAGCAGGGCAAGGAGGTGGGGGAGACG
CTGCTGTACTACGGCTGCCGCCGCTCAGATGAGGACTACCTGTACCGGGAGGAGCTGGCG
CAGTTCCACAGGGACGGTGCGCTCACCCAGCTCAACGTGGCCTTCTCCCGGGAGCAGTCC
CACAAGGTCTACGTCCAGCACCTGCTAAAGCAAGACCGAGAGCACCTGTGGAAGTTGATC
GAAGGCGGTGCCCACATCTACGTCTGTGGGGATGCACGGAACATGGCCAGGGATGTGCAG
AACACCTTCTACGACATCGTGGCTGAGCTCGGGGCCATGGAGCACGCGCAGGCGGTGGAC
TACATCAAGAAACTGATGACCAAGGGCCGCTACTCCCTGGACGTGTGGAGCTAG
|
| Enzyme 3 GenBank Gene ID |
AB051763  |
| Enzyme 3 GeneCard ID |
POR  |
| Enzyme 3 GenAtlas ID |
POR  |
| Enzyme 3 HGNC ID |
HGNC:9208  |
| Enzyme 3 Chromosome Location |
7 |
| Enzyme 3 Locus |
7q11.2 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Shephard EA, Palmer CN, Segall HJ, Phillips IR: Quantification of cytochrome P450 reductase gene expression in human tissues. Arch Biochem Biophys. 1992 Apr;294(1):168-72. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- 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
]
- Haniu M, McManus ME, Birkett DJ, Lee TD, Shively JE: Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites. Biochemistry. 1989 Oct 17;28(21):8639-45. [PubMed
]
- Zhao Q, Modi S, Smith G, Paine M, McDonagh PD, Wolf CR, Tew D, Lian LY, Roberts GC, Driessen HP: Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution. Protein Sci. 1999 Feb;8(2):298-306. [PubMed
]
- Adachi M, Tachibana K, Asakura Y, Yamamoto T, Hanaki K, Oka A: Compound heterozygous mutations of cytochrome P450 oxidoreductase gene (POR) in two patients with Antley-Bixler syndrome. Am J Med Genet A. 2004 Aug 1;128A(4):333-9. [PubMed
]
- Fukami M, Horikawa R, Nagai T, Tanaka T, Naiki Y, Sato N, Okuyama T, Nakai H, Soneda S, Tachibana K, Matsuo N, Sato S, Homma K, Nishimura G, Hasegawa T, Ogata T: Cytochrome P450 oxidoreductase gene mutations and Antley-Bixler syndrome with abnormal genitalia and/or impaired steroidogenesis: molecular and clinical studies in 10 patients. J Clin Endocrinol Metab. 2005 Jan;90(1):414-26. Epub 2004 Oct 13. [PubMed
]
- Arlt W, Walker EA, Draper N, Ivison HE, Ride JP, Hammer F, Chalder SM, Borucka-Mankiewicz M, Hauffa BP, Malunowicz EM, Stewart PM, Shackleton CH: Congenital adrenal hyperplasia caused by mutant P450 oxidoreductase and human androgen synthesis: analytical study. Lancet. 2004 Jun 26;363(9427):2128-35. [PubMed
]
- Fluck CE, Tajima T, Pandey AV, Arlt W, Okuhara K, Verge CF, Jabs EW, Mendonca BB, Fujieda K, Miller WL: Mutant P450 oxidoreductase causes disordered steroidogenesis with and without Antley-Bixler syndrome. Nat Genet. 2004 Mar;36(3):228-30. Epub 2004 Feb 1. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6227 |
| Enzyme 4 Name |
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial |
| Enzyme 4 Synonyms |
- 2-oxoglutarate dehydrogenase complex component E2
- OGDC-E2
- Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- E2K
|
| Enzyme 4 Gene Name |
DLST |
| Enzyme 4 Protein Sequence |
>Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
MLSRSRCVSRAFSRSLSAFQKGNCPLGRRSLPGVSLCQGPGYPNSRKVVINNSVFSVRFF
RTTAVCKDDLVTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAN
GVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPI
PTQMPPVPSPSQPPSGKPVSAVKPTVAPPLAEAGAGKGLRSEHREKMNRMRQRIAQRLKE
AQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNA
VIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELA
IEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVAL
TYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL
|
| Enzyme 4 Number of Residues |
453 |
| Enzyme 4 Molecular Weight |
48728.8 |
| Enzyme 4 Theoretical pI |
9.39 |
| Enzyme 4 GO Classification |
| Function |
- S-acyltransferase activity
- S-succinyltransferase activity
- acyltransferase activity
- catalytic activity
- dihydrolipoyllysine-residue succinyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- tricarboxylic acid cycle
|
| Component |
- macromolecular complex
- oxoglutarate dehydrogenase complex
- protein complex
|
|
| Enzyme 4 General Function |
Involved in acyltransferase activity |
| Enzyme 4 Specific Function |
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components:2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine [RN:R02570]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
4809336  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P36957  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
ODO2_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1362 bp
ATGCTGTCCCGATCCCGCTGTGTGTCTCGGGCGTTCAGCCGCTCGCTCTCCGCCTTCCAG
AAGGGGAACTGCCCTCTAGGGAGACGTTCCCTGCCTGGGGTCTCCTTATGCCAGGGACCA
GGTTACCCTAACAGCAGGAAGGTTGTCATTAACAACAGTGTCTTCAGTGTTCGCTTTTTC
AGAACTACAGCTGTATGCAAGGATGACTTGGTTACAGTCAAAACCCCAGCGTTTGCAGAA
TCTGTCACAGAGGGAGATGTCAGGTGGGAGAAAGCTGTTGGAGACACAGTTGCAGAAGAT
GAAGTGGTTTGTGAGATTGAAACTGACAAGACATCTGTGCAGGTTCCATCACCAGCAAAT
GGCGTGATTGAAGCTCTTTTGGTACCTGATGGGGGAAAAGTCGAAGGAGGCACTCCACTT
TTCACACTCAGGAAAACTGGTGCTGCTCCTGCTAAGGCCAAGCCGGCTGAAGCTCCTGCT
GCTGCAGCCCCAAAAGCAGAACCTACAGCAGCGGCAGTTCCTCCCCCTGCAGCACCCATA
CCCACTCAGATGCCACCGGTGCCCTCGCCCTCACAGCCTCCTTCTGGCAAACCTGTGTCT
GCAGTAAAACCCACTGTTGCCCCACCACTAGCTGAGCCAGGAGCTGGCAAAGGTCTGCGT
TCAGAACATCGGGAGAAAATGAACAGGATGCGGCAGCGCATTGCTCAGCGTCTGAAGGAG
GCCCAGAATACATGTGCAATGCTGACAACTTTTAATGAGATTGACATGAGTAACATCCAG
GAGATGAGGGCTCGGCACAAAGAGGCTTTTTTGAAGAAACATAACCTCAAACTAGGCTTC
ATGTCGGCATTTGTGAAGGCCTCAGCCTTTGCCTTGCAGGAACAGCCTGTTGTAAATGCA
GTGATTGACGACACAACCAAAGAGGTGGTGTATAGGGATTATATTGACATCAGTGTTGCA
GTGGCCACCCCACGGGGTCTGGTGGTTCCAGTCATCAGGAATGTGGAAGCTATGAATTTT
GCAGATATTGAACGGACCATCACTGAACTGGGAGAGAAGGCCCGAAAGAATGAACTTGCC
ATTGAAGATATGGATGGCGGTACCTTCACCATTAGCAATGGAGGCGTTTTTGGCTCGCTC
TTTGGAACACCCATTATCAACCCCCCTCAGTCTGCCATCCTGGGGATGCATGGCATCTTT
GACAGGCCAGTGGCTATAGGAGGCAAGGTAGAGGTGCGGCCCATGATGTACGTGGCACTG
ACCTATGATCACCGGCTGATTGATGGCAGAGAGGCTGTGACTTTCCTCCGCAAAATCAAG
GCAGCGGTAGAGGATCCCAGAGTCCTCCTCCTGGATCTTTAG
|
| Enzyme 4 GenBank Gene ID |
AC006530  |
| Enzyme 4 GeneCard ID |
DLST  |
| Enzyme 4 GenAtlas ID |
DLST  |
| Enzyme 4 HGNC ID |
HGNC:2911  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
14q24.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Nakano K, Matuda S, Sakamoto T, Takase C, Nakagawa S, Ohta S, Ariyama T, Inazawa J, Abe T, Miyata T: Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3. Biochim Biophys Acta. 1993 Dec 14;1216(3):360-8. [PubMed
]
- Nakano K, Takase C, Sakamoto T, Nakagawa S, Inazawa J, Ohta S, Matuda S: Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex. Eur J Biochem. 1994 Aug 15;224(1):179-89. [PubMed
]
- 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
]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
- 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
]
- Xu G, Shin SB, Jaffrey SR: Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19310-5. Epub 2009 Nov 5. [PubMed
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
8590 |
| Enzyme 5 Name |
Glycine cleavage system H protein, mitochondrial |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
GCSH |
| Enzyme 5 Protein Sequence |
>Glycine cleavage system H protein, mitochondrial
MALRVVRSVRALLCTLRAVPLPAAPCPPRPWQLGVGAVRTLRTGPALLSVRKFTEKHEWV
TTENGIGTVGISNFAQEALGDVVYCSLPEVGTKLNKQDEFGALESVKAASELYSPLSGEV
TEINEALAENPGLVNKSCYEDGWLIKMTLSNPSELDELMSEEAYEKYIKSIEE
|
| Enzyme 5 Number of Residues |
173 |
| Enzyme 5 Molecular Weight |
18910.4 |
| Enzyme 5 Theoretical pI |
4.56 |
| Enzyme 5 GO Classification |
| Function |
| — |
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine catabolic process
- glycine decarboxylation via glycine cleavage system
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
- glycine cleavage complex
- intracellular membrane-bounded organelle
- macromolecular complex
- membrane-bounded organelle
- mitochondrion
- organelle
- protein complex
|
|
| Enzyme 5 General Function |
Involved in glycine catabolic process |
| Enzyme 5 Specific Function |
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P23434  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
GCSH_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>522 bp
ATGGCGCTGCGAGTGGTGCGGAGCGTGCGGGCCCTGCTCTGCACCCTGCGCGCGGTCCCG
TTACCCGCCGCGCCCTGCCCGCCGAGGCCCTGGCAGCTGGGGGTGGGCGCCGTCCGTACG
CTGCGCACTGGACCCGCTCTGCTCTCGGTGCGTAAATTCACAGAGAAACACGAATGGGTA
ACAACAGAAAATGGCATTGGAACAGTGGGAATCAGCAATTTTGCACAGGAAGCGTTGGGA
GATGTTGTTTATTGTAGTCTCCCTGAAGTTGGGACAAAATTGAACAAACAAGATGAGTTT
GGTGCTTTGGAAAGTGTGAAAGCTGCTAGTGAACTCTATTCTCCTTTATCAGGAGAAGTA
ACTGAAATTAATGAAGCTCTTGCAGAAAATCCAGGACTTGTAAACAAATCTTGTTATGAA
GATGGTTGGCTGATCAAGATGACACTGAGTAACCCTTCAGAACTAGATGAACTTATGAGT
GAAGAAGCATATGAGAAATACATAAAATCTATTGAGGAGTGA
|
| Enzyme 5 GenBank Gene ID |
M69175  |
| Enzyme 5 GeneCard ID |
GCSH  |
| Enzyme 5 GenAtlas ID |
GCSH  |
| Enzyme 5 HGNC ID |
HGNC:4208  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
16q23.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Koyata H, Hiraga K: The glycine cleavage system: structure of a cDNA encoding human H-protein, and partial characterization of its gene in patients with hyperglycinemias. Am J Hum Genet. 1991 Feb;48(2):351-61. [PubMed
]
- Fujiwara K, Okamura-Ikeda K, Hayasaka K, Motokawa Y: The primary structure of human H-protein of the glycine cleavage system deduced by cDNA cloning. Biochem Biophys Res Commun. 1991 Apr 30;176(2):711-6. [PubMed
]
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
8614 |
| Enzyme 6 Name |
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial |
| Enzyme 6 Synonyms |
- Branched-chain alpha-keto acid dehydrogenase complex component E2
- BCKAD-E2
- BCKADE2
- Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex
- Dihydrolipoamide branched chain transacylase
- Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
|
| Enzyme 6 Gene Name |
DBT |
| Enzyme 6 Protein Sequence |
>Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
MAAVRMLRTWSRNAGKLICVRYFQTCGNVHVLKPNYVCFFGYPSFKYSHPHHFLKTTAAL
RGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKK
LYYNLDDIAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRL
AMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKVEIMPPPPKPKDMTVPIL
VSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEIDLTELVKLREELKPIAFA
RGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVK
NVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTFAKPVIMPPEVAI
GALGSIKAIPRFNQKGEVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD
LK
|
| Enzyme 6 Number of Residues |
482 |
| Enzyme 6 Molecular Weight |
53486.6 |
| Enzyme 6 Theoretical pI |
8.75 |
| Enzyme 6 GO Classification |
| Function |
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity
- protein binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- acyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- fatty-acyl-CoA biosynthetic process
- fatty-acyl-CoA metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in acyltransferase activity |
| Enzyme 6 Specific Function |
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
- 2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine [RN:R02662]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
189053756  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P11182  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
ODB2_HUMAN  |
| Enzyme 6 PDB ID |
1K8O  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1449 bp
ATGGCTGCAGTCCGTATGCTGAGAACCTGGAGCAGGAATGCGGGGAAGCTGATTTGTGTT
CGCTATTTTCAAACATGTGGTAATGTTCATGTTTTGAAGCCAAATTATGTGTGTTTCTTT
GGTTATCCTTCATTCAAGTATAGTCATCCACATCACTTCCTGAAAACAACTGCTGCTCTC
CGTGGACAGGTTGTTCAGTTCAAGCTCTCAGACATTGGAGAAGGGATTAGAGAAGTAACT
GTTAAAGAATGGTATGTAAAAGAAGGAGATACAGTGTCTCAGTTTGATAGCATCTGTGAA
GTTCAAAGTGATAAAGCTTCTGTTACCATCACTAGTCGTTATGATGGAGTCATTAAAAAA
CTCTATTATAATCTAGACGATATTGCCTATGTGGGGAAGCCATTAGTAGACATAGAAACG
GAAGCTTTAAAAGATTCAGAAGAAGATGTTGTTGAAACTCCTGCAGTGTCTCATGATGAA
CATACACACCAAGAGATAAAGGGCCGAAAAACACTGGCAACTCCTGCAGTTCGCCGTCTG
GCAATGGAAAACAATATTAAGCTGAGTGAAGTTGTTGGCTCAGGAAAAGATGGCAGAATA
CTTAAAGAAGATATCCTCAACTATTTGGAAAAGCAGACAGGAGCTATATTGCCTCCTTCA
CCCAAAGTTGAAATTATGCCACCTCCACCAAAGCCAAAAGACATGACTGTTCCTATACTA
GTATCAAAACCTCCGGTATTCACAGGCAAAGACAAAACAGAACCCATAAAAGGCTTTCAA
AAAGCAATGGTCAAGACTATGTCTGCAGCCCTGAAGATACCTCATTTTGGTTATTGTGAT
GAGATTGACCTTACTGAACTGGTTAAGCTCCGAGAAGAATTAAAACCCATTGCATTTGCT
CGTGGAATTAAACTCTCCTTTATGCCTTTCTTCTTAAAGGCTGCTTCCTTGGGATTACTA
CAGTTTCCTATCCTTAACGCTTCTGTGGATGAAAACTGCCAGAATATAACATATAAGGCT
TCTCATAACATTGGGATAGCAATGGATACTGAGCAGGGTTTGATTGTCCCTAATGTGAAA
AATGTTCAGATCTGCTCTATATTTGACATCGCCACTGAACTGAACCGCCTCCAGAAATTG
GGCTCTGTGGGTCAGCTCAGCACCACTGATCTTACAGGAGGAACATTTACTCTTTCCAAC
ATTGGATCAATTGGTGGTACCTTTGCCAAACCAGTGATAATGCCACCTGAAGTAGCCATT
GGGGCCCTTGGATCAATTAAGGCCATTCCCCGATTTAACCAGAAAGGAGAAGTATATAAG
GCACAGATAATGAATGTGAGCTGGTCAGCTGATCACAGAGTTATTGATGGTGCTACAATG
TCACGCTTCTCCAATTTGTGGAAATCCTATTTAGAAAACCCAGCTTTTATGCTACTAGAT
CTGAAATGA
|
| Enzyme 6 GenBank Gene ID |
AK313191  |
| Enzyme 6 GeneCard ID |
DBT  |
| Enzyme 6 GenAtlas ID |
DBT  |
| Enzyme 6 HGNC ID |
HGNC:2698  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
1p31 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Lau KS, Chuang JL, Herring WJ, Danner DJ, Cox RP, Chuang DT: The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex. Biochim Biophys Acta. 1992 Oct 20;1132(3):319-21. [PubMed
]
- Hummel KB, Litwer S, Bradford AP, Aitken A, Danner DJ, Yeaman SJ: Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure. J Biol Chem. 1988 May 5;263(13):6165-8. [PubMed
]
- Danner DJ, Litwer S, Herring WJ, Pruckler J: Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase. J Biol Chem. 1989 May 5;264(13):7742-6. [PubMed
]
- Nobukuni Y, Mitsubuchi H, Endo F, Matsuda I: Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex. Biochem Biophys Res Commun. 1989 Jun 30;161(3):1035-41. [PubMed
]
- 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
]
- 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
]
- 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
]
- Lau KS, Griffin TA, Hu CW, Chuang DT: Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. Biochemistry. 1988 Mar 22;27(6):1972-81. [PubMed
]
- Lau KS, Herring WJ, Chuang JL, McKean M, Danner DJ, Cox RP, Chuang DT: Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene. J Biol Chem. 1992 Nov 25;267(33):24090-6. [PubMed
]
- Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed
]
- 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
]
- Chang CF, Chou HT, Chuang JL, Chuang DT, Huang TH: Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex. J Biol Chem. 2002 May 3;277(18):15865-73. Epub 2002 Feb 11. [PubMed
]
- Fisher CW, Lau KS, Fisher CR, Wynn RM, Cox RP, Chuang DT: A 17-bp insertion and a Phe215----Cys missense mutation in the dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive maple syrup urine disease patient WG-34. Biochem Biophys Res Commun. 1991 Jan 31;174(2):804-9. [PubMed
]
- Tsuruta M, Mitsubuchi H, Mardy S, Miura Y, Hayashida Y, Kinugasa A, Ishitsu T, Matsuda I, Indo Y: Molecular basis of intermittent maple syrup urine disease: novel mutations in the E2 gene of the branched-chain alpha-keto acid dehydrogenase complex. J Hum Genet. 1998;43(2):91-100. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
14991 |
| Enzyme 7 Name |
3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial |
| Enzyme 7 Synonyms |
- Beta-ketoacyl-ACP synthase
|
| Enzyme 7 Gene Name |
OXSM |
| Enzyme 7 Protein Sequence |
>3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
MSNCLQNFLKITSTRLLCSRLCQQLRSKRKFFGTVPISRLHRRVVITGIGLVTPLGVGTH
LVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSDEGQFNEQNFVSKSDIKSMSSPTI
MAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFV
PKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCI
SPLSLAGFSRARALSTNSDPKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYA
EVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN
KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF
DLNYVPLKAQEWKTEKRFIGLTNSFGFGGTNATLCIAGL
|
| Enzyme 7 Number of Residues |
459 |
| Enzyme 7 Molecular Weight |
48842.4 |
| Enzyme 7 Theoretical pI |
7.72 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- biosynthetic process
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid biosynthetic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in catalytic activity |
| Enzyme 7 Specific Function |
May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
- an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] [RN:R02768]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
7020821  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9NWU1  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
OXSM_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1380 bp
ATGTCCAACTGCCTGCAAAATTTCCTGAAAATTACAAGCACTCGTCTTCTATGTTCAAGA
TTATGCCAACAGTTAAGAAGTAAAAGGAAGTTTTTCGGAACTGTGCCAATATCCAGATTG
CATAGGCGAGTTGTCATTACAGGCATTGGCTTAGTGACTCCTCTTGGTGTTGGAACTCAC
CTGGTTTGGGATCGTCTTATCGGAGGAGAGAGTGGAATTGTTTCACTGGTTGGTGAAGAG
TATAAGAGTATCCCTTGCAGTGTTGCTGCTTATGTGCCAAGAGGTAGTGATGAAGGTCAG
TTCAATGAACAAAACTTTGTGTCCAAATCAGATATCAAGTCCATGTCTTCTCCCACCATC
ATGGCCATTGGGGCTGCAGAATTAGCCATGAAGGATTCTGGCTGGCATCCTCAGTCAGAA
GCTGATCAAGTGGCTACTGGTGTTGCAATTGGCATGGGAATGATTCCTCTTGAAGTTGTT
TCTGAAACTGCTTTGAATTTTCAGACAAAAGGTTACAATAAAGTTAGCCCATTTTTTGTC
CCTAAGATTCTGGTCAATATGGCAGCAGGCCAGGTCAGCATTCGATATAAACTCAAGGGC
CCAAATCATGCAGTATCCACAGCCTGTACCACAGGAGCTCATGCTGTGGGAGACTCATTT
AGATTTATAGCCCATGGTGATGCTGATGTGATGGTGGCTGGAGGTACAGATTCTTGTATT
AGCCCTTTATCTCTTGCTGGGTTTTCCAGAGCCCGGGCTCTGAGCACAAACTCAGATCCC
AAGTTGGCATGTCGACCATTTCATCCAAAGAGAGATGGTTTTGTAATGGGAGAAGGTGCA
GCTGTGCTGGTGCTGGAAGAATATGAACATGCTGTTCAAAGAAGAGCCCGGATCTATGCA
GAAGTTTTGGGCTATGGACTCTCAGGTGATGCTGGTCACATAACTGCCCCTGATCCTGAA
GGAGAAGGTGCCTTAAGGTGTATGGCTGCTGCTTTAAAAGATGCAGGTGTGCAGCCTGAG
GAGATATCCTATATCAATGCACATGCTACTTCCACACCATTGGGAGATGCTGCTGAAAAC
AAAGCTATCAAACATCTCTTCAAAGACCATGCATATGCCCTTGCAGTTTCCTCAACTAAG
GGAGCAACAGGACATCTGCTGGGAGCTGCAGGGGCAGTCGAGGCAGCTTTTACCACATTA
GCTTGTTATTATCAAAAACTACCACCTACTTTAAACCTGGATTGTTCGGAACCAGAATTT
GATCTCAACTATGTTCCACTAAAGGCACAGGAATGGAAAACTGAGAAAAGATTTATTGGC
CTCACCAATTCCTTTGGTTTTGGTGGTACTAATGCAACACTTTGTATTGCTGGACTGTAG
|
| Enzyme 7 GenBank Gene ID |
AK000611  |
| Enzyme 7 GeneCard ID |
OXSM  |
| Enzyme 7 GenAtlas ID |
OXSM  |
| Enzyme 7 HGNC ID |
HGNC:26063  |
| Enzyme 7 Chromosome Location |
3 |
| Enzyme 7 Locus |
3p24.2 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
- 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
]
- Zhang L, Joshi AK, Hofmann J, Schweizer E, Smith S: Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain. J Biol Chem. 2005 Apr 1;280(13):12422-9. Epub 2005 Jan 24. [PubMed
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
16938 |
| Enzyme 8 Name |
Lipoyltransferase 1, mitochondrial |
| Enzyme 8 Synonyms |
- Lipoate biosynthesis protein
- Lipoate-protein ligase
- Lipoyl ligase
|
| Enzyme 8 Gene Name |
LIPT1 |
| Enzyme 8 Protein Sequence |
>Lipoyltransferase 1, mitochondrial
MLIPFSMKNCFQLLCNCQVPAAGFKKTVKNGLILQSISNDVYQNLAVEDWIHDHMNLEGK
PILFFWQNSPSVVIGRHQNPWQECNLNLMREEGIKLARRRSGGGTVYHDMGNINLTFFTT
KKKYDRMENLKLIVRALNAVQPQLDVQATKRFDLLLDGQFKISGTASKIGRTTAYHHCTL
LCSTDGTFLSSLLKSPYQGIRSNATASIPSLVKNLLEKDPTLTCEVLMNAVATEYAAYHQ
IDNHIHLINPTDETLFPGINSKAKELQTWEWIYGKTPKFSINTSFHVLYEQSHLEIKVFI
DIKNGRIEICNIEAPDHWLPLEIRDKLNSSLIGSKFCPTETTMLTNILLRTCPQDHKLNS
KWNILCEKIKGIM
|
| Enzyme 8 Number of Residues |
373 |
| Enzyme 8 Molecular Weight |
42478.8 |
| Enzyme 8 Theoretical pI |
8.48 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- transferase activity
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein lipoylation
- protein modification process
- protein-cofactor linkage
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in catalytic activity |
| Enzyme 8 Specific Function |
Catalyzes the transfer of the lipoyl group from lipoyl- AMP to the specific lysine residue of lipoyl domains of lipoate- dependent enzymes |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q9Y234  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
LIPT_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1122 bp
ATGCTGATCCCATTTTCAATGAAGAATTGCTTCCAGTTACTTTGTAACTGCCAGGTCCCA
GCAGCTGGCTTTAAAAAAACAGTAAAAAATGGGCTCATTTTACAGTCAATTTCCAATGAT
GTCTATCAAAATCTGGCTGTGGAAGACTGGATCCATGACCATATGAATCTAGAAGGCAAA
CCAATTCTATTCTTTTGGCAGAATTCTCCCTCTGTTGTAATTGGTAGGCATCAAAATCCT
TGGCAGGAATGTAACCTGAATCTAATGAGAGAAGAAGGTATAAAACTGGCTCGGAGAAGA
AGTGGAGGAGGAACAGTCTACCATGATATGGGTAATATCAATTTGACTTTCTTTACAACC
AAAAAAAAGTATGATAGAATGGAAAATCTGAAATTAATTGTGAGAGCTCTGAATGCTGTC
CAACCCCAGCTGGATGTGCAGGCTACCAAAAGATTTGACCTTTTACTTGATGGACAGTTT
AAAATCTCAGGAACAGCTTCTAAGATCGGCCGGACTACTGCCTATCACCATTGCACTTTA
TTATGTAGTACTGATGGGACGTTCCTGTCTTCTTTGCTAAAGAGCCCTTACCAAGGGATC
AGGAGCAATGCCACTGCTAGCATACCTTCCTTAGTGAAAAATCTTTTGGAAAAGGATCCC
ACTCTGACCTGTGAAGTACTAATGAATGCTGTTGCTACAGAGTATGCTGCCTATCATCAA
ATTGATAATCACATTCACCTAATAAACCCAACGGATGAGACACTGTTTCCTGGAATAAAT
AGCAAAGCCAAAGAACTGCAAACTTGGGAGTGGATATATGGCAAAACTCCAAAGTTTAGT
ATAAATACTTCCTTTCATGTGTTATATGAACAGTCACACTTGGAAATTAAAGTATTCATA
GACATAAAGAATGGAAGAATTGAAATTTGTAATATTGAAGCACCTGATCATTGGTTGCCA
TTGGAAATACGTGACAAATTAAATTCAAGTCTTATTGGCAGTAAGTTTTGCCCAACTGAA
ACTACCATGCTAACAAATATATTACTTAGAACATGTCCACAAGACCACAAACTAAACAGT
AAATGGAATATTCTCTGTGAAAAAATTAAGGGAATAATGTGA
|
| Enzyme 8 GenBank Gene ID |
AB017566  |
| Enzyme 8 GeneCard ID |
LIPT1  |
| Enzyme 8 GenAtlas ID |
LIPT1  |
| Enzyme 8 HGNC ID |
HGNC:29569  |
| Enzyme 8 Chromosome Location |
2 |
| Enzyme 8 Locus |
2q11.2 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y: Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene. Eur J Biochem. 1999 Mar;260(3):761-7. [PubMed
]
- 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
]
- 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
]
|
| Enzyme 8 Metabolite References |
Not Available |