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Human Metabolome Database Version 2.5

 

Showing metabocard for N-Acetyl-L-tyrosine (HMDB00866)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2011-06-14 17:02:28
Accession Number HMDB00866
Secondary Accession Numbers Not Available
Common Name N-Acetyl-L-tyrosine
Description Acetyltyrosine is a side chain reaction of tyrosine. It converts to tyrosine and then can be used in neurotransmitter treatment as a precursor of cathecholamine (http://www.neuroassist.com/).
Synonyms
  1. (2S)-2-Acetylamino-3-(4-hydroxyphenyl)propanoate
  2. (2S)-2-Acetylamino-3-(4-hydroxyphenyl)propanoic acid
  3. L-N-Acetyltyrosine
  4. L-N-acetyl-Tyrosine
  5. N-Acetyl-L-tyrosine
  6. N-Acetyl-tyrosine
  7. N-Acetyltyrosine
  8. N-acetyl-4-hydroxyphenylalanine
Chemical IUPAC Name 2-acetylamino-3-(4-hydroxyphenyl)-propanoic acid
Chemical Formula C11H13NO4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • phenol or hydroxyhetarene
  • carboxylic acid
  • secondary carboxylic acid amide
  • aromatic compound
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 223.225
Monoisotopic Molecular Weight 223.084457
Isomeric SMILES CC(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O
Canonical SMILES CC(=O)NC(CC1=CC=C(O)C=C1)C(O)=O
KEGG Compound ID C01657 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00866 Link Image
Metagene Link HMDB00866 Link Image
METLIN ID Not Available
PubChem Compound 68310 Link Image
PubChem Substance 3154274 Link Image
ChEBI ID 28828 Link Image
CAS Registry Number 537-55-3
InChI Identifier InChI=1/C11H13NO4/c1-7(13)12-10(11(15)16)6-8-2-4-9(14)5-3-8/h2-5,10,14H,6H2,1H3,(H,12,13)(H,15,16)/t10-/m0/s1
Synthesis Reference Liu, Aifu. Preparation of N-acetyl-L-tyrosine. Faming Zhuanli Shenqing Gongkai Shuomingshu (2005), 5 pp.
Melting Point (Experimental) 149 - 152 oC
Experimental Water Solubility 297 mg/mL [HMP expt] Source: PhysProp
Predicted Water Solubility 9.38 mg/mL [MEYLAN,WM et al. (1996)]; 2.51 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.03 [Predicted by ALOGPS]; -1.5 [Predicted by PubChem via XLOGP]; 1.48 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from Solubility)
Biofluid Location
  • Blood
  • Urine
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal)
Biofluid Blood
Value 331.0 +/- 74.0 uM
Age Newborn:0-30 days old
Sex Both
Condition Preterm birth
Comments Not Available
References
  • Van Goudoever JB, Sulkers EJ, Timmerman M, Huijmans JG, Langer K, Carnielli VP, Sauer PJ: Amino acid solutions for premature neonates during the first week of life: the role of N-acetyl-L-cysteine and N-acetyl-L-tyrosine. JPEN J Parenter Enteral Nutr. 1994 Sep-Oct;18(5):404-8. [PubMed Link Image]
Biofluid Urine
Value 10 +/- 2 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Male
Condition Aromatic L-amino acid decarboxylase deficiency
Comments Not Available
References
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Biofluid Urine
Value 1.00 (0.00-2.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Tyrosinemia I
Comments Not Available
References
Biofluid Urine
Value 115.00 (30.00-200.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Tyrosinemia I
Comments Not Available
References
Associated Disorders
Condition References
Aromatic L-amino acid decarboxylase deficiency
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Preterm birth
  • Van Goudoever JB, Sulkers EJ, Timmerman M, Huijmans JG, Langer K, Carnielli VP, Sauer PJ: Amino acid solutions for premature neonates during the first week of life: the role of N-acetyl-L-cysteine and N-acetyl-L-tyrosine. JPEN J Parenter Enteral Nutr. 1994 Sep-Oct;18(5):404-8. [PubMed Link Image]
Tyrosinemia I
OMIM ID
  • 107930 Link Image (Aromatic L-amino acid decarboxylase deficiency)
  • 276700 Link Image (Tyrosinemia I)
Pathways Not Available
General References
  1. Rao NR, Bhat PG, Pattabiraman TN: Estimation of serum alpha 2-macroglobulin based on the esterolytic activity of bound alpha-chymotrypsin. Biochem Med. 1984 Dec;32(3):357-63. [PubMed Link Image]
  2. Hoffer LJ, Sher K, Saboohi F, Bernier P, MacNamara EM, Rinzler D: N-acetyl-L-tyrosine as a tyrosine source in adult parenteral nutrition. JPEN J Parenter Enteral Nutr. 2003 Nov-Dec;27(6):419-22. [PubMed Link Image]
  3. Dietze EC, Grillo MP, Kalhorn T, Nieslanik BS, Jochheim CM, Atkins WM: Thiol ester hydrolysis catalyzed by glutathione S-transferase A1-1. Biochemistry. 1998 Oct 20;37(42):14948-57. [PubMed Link Image]
  4. Druml W, Hubl W, Roth E, Lochs H: Utilization of tyrosine-containing dipeptides and N-acetyl-tyrosine in hepatic failure. Hepatology. 1995 Apr;21(4):923-8. [PubMed Link Image]
  5. Van Goudoever JB, Sulkers EJ, Timmerman M, Huijmans JG, Langer K, Carnielli VP, Sauer PJ: Amino acid solutions for premature neonates during the first week of life: the role of N-acetyl-L-cysteine and N-acetyl-L-tyrosine. JPEN J Parenter Enteral Nutr. 1994 Sep-Oct;18(5):404-8. [PubMed Link Image]
  6. Drabik G, Naskalski JW: Chlorination of N-acetyltyrosine with HOCl, chloramines, and myeloperoxidase-hydrogen peroxide-chloride system. Acta Biochim Pol. 2001;48(1):271-5. [PubMed Link Image]
  7. Fu S, Wang H, Davies M, Dean R: Reactions of hypochlorous acid with tyrosine and peptidyl-tyrosyl residues give dichlorinated and aldehydic products in addition to 3-chlorotyrosine. J Biol Chem. 2000 Apr 14;275(15):10851-8. [PubMed Link Image]
Metabolic Enzymes
  1. Glycine N-acyltransferase
  2. Glycine N-acyltransferase-like protein 1
  3. Glycine N-acyltransferase-like protein 2
Enzyme 1 [top]
Enzyme 1 ID 12971
Enzyme 1 Name Glycine N-acyltransferase
Enzyme 1 Synonyms
  1. Acyl-CoA:glycine N-acyltransferase
  2. AAc
  3. Aralkyl acyl-CoA N-acyltransferase
  4. Aralkyl acyl-CoA:amino acid N-acyltransferase
  5. HRP-1(CLP)
Enzyme 1 Gene Name GLYAT
Enzyme 1 Protein Sequence >Glycine N-acyltransferase
MMLPLQGAQMLQMLEKSLRKSLPASLKVYGTVFHINHGNPFNLKAVVDKWPDFNTVVVCP
QEQDMTDDLDHYTNTYQIYSKDPQNCQEFLGSPELINWKQHLQIQSSQPSLNEAIQNLAA
IKSFKVKQTQRILYMAAETAKELTPFLLKSKILSPSGGKPKAINQEMFKLSSMDVTHAHL
VNKFWHFGGNERSQRFIERCIQTFPTCCLLGPEGTPVCWDLMDQTGEMRMAGTLPEYRLH
GLVTYVIYSHAQKLGKLGFPVYSHVDYSNEAMQKMSYTLQHVPIPRSWNQWNCVPL
Enzyme 1 Number of Residues 296
Enzyme 1 Molecular Weight 33897.0
Enzyme 1 Theoretical pI 8.28
Enzyme 1 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycine N-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 1 General Function Involved in glycine N-acyltransferase activity
Enzyme 1 Specific Function Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • acyl-CoA + glycine = CoA + N-acylglycine [RN:R00395]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 111038137 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q6IB77 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GLYAT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >891 bp
ATGATGTTACCATTGCAAGGTGCCCAGATGCTGCAGATGCTGGAGAAATCCTTGAGGAAG
AGCCTCCCAGCATCCTTAAAGGTTTATGGAACTGTCTTTCACATAAACCATGGAAATCCA
TTCAATCTGAAGGCTGTGGTGGACAAGTGGCCTGATTTTAATACAGTGGTTGTCTGCCCT
CAGGAGCAGGATATGACAGATGACCTTGATCACTATACCAATACTTACCAAATCTACTCC
AAAGATCCCCAAAACTGTCAGGAATTCCTTGGATCACCAGAACTCATCAACTGGAAACAG
CATTTACAGATTCAAAGTTCACAGCCTAGCCTGAATGAGGCTATACAAAATCTTGCAGCC
ATTAAGTCCTTCAAAGTCAAACAAACACAACGCATTCTCTATATGGCAGCTGAAACAGCC
AAGGAACTGACTCCTTTCCTGCTGAAATCAAAGATTTTATCTCCCAATGGTGGCAAACCC
AAGGCCATCAACCAAGAGATGTTTAAACTCTCATCCATGGATGTTACCCATGCTCACTTG
GTGAATAAATTCTGGCATTTTGGTGGTAATGAGAGGAGCCAGAGATTCATTGAGCGCTGC
ATTCAGACCTTTCCCACCTGCTGTCTCCTGGGGCCTGAGGGGACCCCTGTGTGCTGGGAT
CTAATGGACCAGACTGGAGAGATGAGAATGGCAGGCACCTTGCCGGAATACCGGCTCCAT
GGCCTTGTGACGTATGTCATCTATTCCCACGCCCAGAAATTGGGCAAACTTGGGTTTCCT
GTCTATTCTCATGTAGACTACAGCAATGAAGCTATGCAAAAAATGAGTTACACACTGCAA
CATGTTCCCATTCCCAGAAGCTGGAACCAGTGGAACTGTGTACCTCTGTGA
Enzyme 1 GenBank Gene ID NM_201648.2 Link Image
Enzyme 1 GeneCard ID GLYAT Link Image
Enzyme 1 GenAtlas ID GLYAT Link Image
Enzyme 1 HGNC ID HGNC:13734 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 11q12.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. van der Westhuizen FH, Pretorius PJ, Erasmus E: The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase. J Biochem Mol Toxicol. 2000;14(2):102-9. [PubMed Link Image]
  2. 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 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. Mawal YR, Qureshi IA: Purification to homogeneity of mitochondrial acyl coa:glycine n-acyltransferase from human liver. Biochem Biophys Res Commun. 1994 Dec 15;205(2):1373-9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 12972
Enzyme 2 Name Glycine N-acyltransferase-like protein 1
Enzyme 2 Synonyms
  1. Acyl-CoA:glycine N-acyltransferase-like protein 1
Enzyme 2 Gene Name GLYATL1
Enzyme 2 Protein Sequence >Glycine N-acyltransferase-like protein 1
MILLNNSHKLLALYKSLARSIPESLKVYGSVYHINHGNPFNMEVLVDSWPEYQMVIIRPQ
KQEMTDDMDSYTNVYRMFSKEPQKSEEVLKNCEIVNWKQRLQIQGLQESLGEGIRVATFS
KSVKVEHSRALLLVTEDILKLNASSKSKLGSWAETGHPDDEFESETPNFKYAQLDVSYSG
LVNDNWKRGKNERSLHYIKRCIEDLPAACMLGPEGVPVSWVTMDPSCEVGMAYSMEKYRR
TGNMARVMVRYMKYLRQKNIPFYISVLEENEDSRRFVGQFGFFEASCEWHQWTCYPQNLV
PF
Enzyme 2 Number of Residues 302
Enzyme 2 Molecular Weight 35100.9
Enzyme 2 Theoretical pI 6.86
Enzyme 2 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycine N-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 2 General Function Involved in glycine N-acyltransferase activity
Enzyme 2 Specific Function Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • acyl-CoA + glycine = CoA + N-acylglycine [RN:R00395]
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 Q969I3 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GLYL1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >909 bp
ATGATCCTACTGAATAACTCCCATAAGCTGCTGGCCCTATACAAATCCTTGGCCAGGAGC
ATCCCTGAGTCCCTGAAGGTGTATGGCTCTGTGTATCACATCAATCACGGGAACCCCTTC
AACATGGAGGTGCTGGTGGATTCCTGGCCTGAATATCAGATGGTTATTATCCGGCCTCAA
AAGCAGGAGATGACTGATGACATGGATTCATACACAAACGTATATCGTATGTTCTCCAAA
GAGCCTCAAAAATCAGAAGAAGTTTTGAAAAATTGTGAGATCGTAAACTGGAAACAGAGA
CTCCAAATCCAAGGTCTTCAAGAAAGTTTAGGTGAGGGGATAAGAGTGGCTACATTTTCA
AAGTCAGTGAAAGTAGAGCATTCGAGAGCACTCCTCTTGGTTACGGAAGATATTCTGAAG
CTCAATGCCTCCAGTAAAAGCAAGCTTGGAAGCTGGGCTGAGACAGGCCACCCAGATGAT
GAATTTGAAAGTGAAACTCCCAACTTTAAGTATGCCCAGCTGGATGTCTCTTATTCTGGG
CTGGTAAATGACAACTGGAAGCGAGGGAAGAATGAGAGGAGCCTGCATTACATCAAGCGC
TGCATAGAAGACCTGCCAGCAGCCTGTATGCTCGGCCCAGAGGGAGTCCCGGTCTCATGG
GTAACCATGGACCCTTCTTGTGAAGTAGGAATGGCCTACAGCATGGAAAAATACCGAAGG
ACAGGCAACATGGCACGAGTGATGGTGCGATACATGAAATATCTGCGTCAGAAGAATATT
CCATTTTACATCTCTGTGTTGGAAGAAAATGAAGACTCCCGCAGATTTGTGGGGCAGTTT
GGTTTCTTTGAGGCCTCCTGTGAGTGGCACCAATGGACTTGCTACCCACAGAATCTAGTT
CCATTTTAG
Enzyme 2 GenBank Gene ID DQ084381 Link Image
Enzyme 2 GeneCard ID GLYATL1 Link Image
Enzyme 2 GenAtlas ID GLYATL1 Link Image
Enzyme 2 HGNC ID HGNC:30519 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 11q12.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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]
  2. 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 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 12973
Enzyme 3 Name Glycine N-acyltransferase-like protein 2
Enzyme 3 Synonyms
  1. Acyl-CoA:glycine N-acyltransferase-like protein 2
Enzyme 3 Gene Name GLYATL2
Enzyme 3 Protein Sequence >Glycine N-acyltransferase-like protein 2
MLVLHNSQKLQILYKSLEKSIPESIKVYGAIFNIKDKNPFNMEVLVDAWPDYQIVITRPQ
KQEMKDDQDHYTNTYHIFTKAPDKLEEVLSYSNVISWEQTLQIQGCQEGLDEAIRKVATS
KSVQVDYMKTILFIPELPKKHKTSSNDKMELFEVDDDNKEGNFSNMFLDASHAGLVNEHW
AFGKNERSLKYIERCLQDFLGFGVLGPEGQLVSWIVMEQSCELRMGYTVPKYRHQGNMLQ
IGYHLEKYLSQKEIPFYFHVADNNEKSLQALNNLGFKICPCGWHQWKCTPKKYC
Enzyme 3 Number of Residues 294
Enzyme 3 Molecular Weight 34277.1
Enzyme 3 Theoretical pI 6.67
Enzyme 3 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycine N-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 3 General Function Involved in glycine N-acyltransferase activity
Enzyme 3 Specific Function Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • acyl-CoA + glycine = CoA + N-acylglycine [RN:R00395]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 29243559 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8WU03 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GLYL2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >885 bp
ATGCTTGTGCTTCATAACTCTCAGAAGCTGCAGATTCTGTATAAATCCTTAGAAAAGAGC
ATCCCTGAATCCATAAAGGTATATGGCGCCATTTTCAACATAAAAGATAAAAACCCTTTC
AACATGGAGGTGCTGGTAGATGCCTGGCCAGATTACCAGATCGTCATTACCCGGCCTCAG
AAACAGGAGATGAAAGATGACCAGGATCATTATACCAACACTTACCACATCTTCACCAAA
GCTCCTGACAAATTAGAGGAAGTCCTGTCATACTCCAATGTAATCAGCTGGGAGCAAACT
TTGCAGATCCAAGGTTGCCAAGAGGGCTTGGATGAAGCAATAAGAAAGGTTGCAACTTCA
AAATCAGTGCAGGTAGATTACATGAAAACCATCCTCTTTATACCGGAATTACCAAAGAAA
CACAAGACCTCAAGTAATGACAAGATGGAGTTATTTGAAGTGGATGATGATAACAAGAAA
GGAAACTTTTCAAACATGTTCTTAGATGCTTCACATGCAGGTCTTGTGAATGAACACTGG
GCCTTTGGGAAAAATGAGAGGAGCTTGAAATATATTGAACGCTGCCTCCAGGATTTTCTA
GGATTTGGCGTGCTGGGTCCAGAGGGCCAGCTTGTCTCTTGGATTGTGATGGAACGGTCC
TGTGAGTTGAGAATGGGTTATACTGTCCCCAAATACAGACACCAAGGCAACATGTTGCAA
ATTGGTTACCATCTTGAAAAGTATCTTTCTCAGAAAGAAATCCCATTTTATTTCCATGTG
GCAGATAATAATGAGAAAAGCCTACAGGCACTGAACAATTTGGGGTTTAAGATTTGTCCC
TGTGGCTGGCATCAGTGGAAATGCACCCCCAAGAAATGTTGTTGA
Enzyme 3 GenBank Gene ID AF426250 Link Image
Enzyme 3 GeneCard ID GLYATL2 Link Image
Enzyme 3 GenAtlas ID GLYATL2 Link Image
Enzyme 3 HGNC ID HGNC:24178 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 11q12.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available