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Human Metabolome Database Version 2.5

 

Showing metabocard for Lithocholic acid glycine conjugate (HMDB00698)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-07-13 12:15:12
Accession Number HMDB00698
Secondary Accession Numbers HMDB02474
Common Name Lithocholic acid glycine conjugate
Description Lithocholic acid glycine conjugate is an acyl glycine and a bile acid-glycine conjugate. is an acyl glycine and a bile acid-glycine conjugate. It is a secondary bile acid produced by the action of enzymes existing in the microbial flora of the colonic environment. In hepatocytes, both primary and secondary bile acids undergo amino acid conjugation at the C-24 carboxylic acid on the side chain, and almost all bile acids in the bile duct therefore exist in a glycine conjugated form (PMID:16949895). Bile acids are steroid acids found predominantly in bile of mammals. The distinction between different bile acids is minute, depends only on presence or absence of hydroxyl groups on positions 3, 7, and 12. Bile acids are physiological detergents that facilitate excretion, absorption, and transport of fats and sterols in the intestine and liver. Bile acids are also steroidal amphipathic molecules derived from the catabolism of cholesterol. They modulate bile flow and lipid secretion, are essential for the absorption of dietary fats and vitamins, and have been implicated in the regulation of all the key enzymes involved in cholesterol homeostasis. Bile acids recirculate through the liver, bile ducts, small intestine and portal vein to form an enterohepatic circuit. They exist as anions at physiological pH and, consequently, require a carrier for transport across the membranes of the enterohepatic tissues. The unique detergent properties of bile acids are essential for the digestion and intestinal absorption of hydrophobic nutrients. Bile acids have potent toxic properties (e.g., membrane disruption) and there are a plethora of mechanisms to limit their accumulation in blood and tissues. (PMID: 11316487, 16037564, 12576301, 11907135)
Synonyms
  1. 3a-Hydroxy-5b-cholanic acid glycine ester
  2. 3a-Hydroxy-5b-cholanoylglycine
  3. 3a-Hydroxy-N-(carboxymethyl)-5b-cholan-24-amide
  4. Glycolithocholic acid
  5. Lithocholic acid glycine conjugate
  6. Lithocholic acid glycine conjugic acid
  7. Lithocholylglycine
  8. N-(3a-Hydroxy-5b-cholanoyl)glycine
  9. N-(3a-hydroxy-5b-cholan-24-oyl)-Glycine
  10. N-(carboxymethyl)-3a-hydroxy-5b-Cholan-24-amide
  11. glycolithocholate
  12. lithocholoyglycine
  13. 3alpha-hydroxy-5beta-cholan-24-oic acid N-(carboxymethyl)amide
  14. 3alpha-hydroxy-5beta-cholan-24-oate
  15. 3alpha-hydroxy-5beta-cholan-24-oic acid
Chemical IUPAC Name N-[(3a,5b)-3-hydroxy-24-oxocholan-24-yl]-(9CI) Glycine
Chemical Formula C26H43NO4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Bile Acids
  • Acyl Glycines
Sub Class
  • Bile-acid glycine conjugates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid
  • secondary carboxylic acid amide
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 433.624
Monoisotopic Molecular Weight 433.319214
Isomeric SMILES C[C@H](CCC(=O)NCC(O)=O)[C@H]1CC[C@H]2[C@@H]3CC[C@@H]4C[C@H](O)CC[C@]4(C)[C@H]3CC[C@]12C
Canonical SMILES CC(CCC(=O)NCC(O)=O)C1CCC2C3CCC4CC(O)CCC4(C)C3CCC12C
KEGG Compound ID Not Available
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00698 Link Image
Metagene Link HMDB00698 Link Image
METLIN ID 5666 Link Image
PubChem Compound 115245 Link Image
PubChem Substance 692226 Link Image
ChEBI ID Not Available
CAS Registry Number 474-74-8
InChI Identifier InChI=1/C26H43NO4/c1-16(4-9-23(29)27-15-24(30)31)20-7-8-21-19-6-5-17-14-18(28)10-12-25(17,2)22(19)11-13-26(20,21)3/h16-22,28H,4-15H2,1-3H3,(H,27,29)(H,30,31)/t16-,17-,18-,19+,20-,21+,22+,25+,26-/m1/s1
Synthesis Reference Momose, Toshiaki; Tsubaki, Takayuki; Iida, Takashi; Nambara, Toshio. An improved synthesis of taurine- and glycine-conjugated bile acids. Lipids (1997), 32(7), 775-778.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.53e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 3.71 [Predicted by ALOGPS]; 3.6 [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 Not Available
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
  • Membrane (Predicted from LogP)
Biofluid Location
  • Bile
  • Blood
Tissue Location
Tissue References
Gall Bladder
Intestine
Kidney
Liver
Concentrations (Normal)
Biofluid Bile
Value 620 (590-650) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tadano T, Kanoh M, Matsumoto M, Sakamoto K, Kamano T: Studies of serum and feces bile acids determination by gas chromatography-mass spectrometry. Rinsho Byori. 2006 Feb;54(2):103-10. [PubMed Link Image]
Biofluid Blood
Value 0.009 (0.005-0.015) uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Wang J, Joy T, Mymin D, Frohlich J, Hegele RA: Phenotypic heterogeneity of sitosterolemia. J Lipid Res. 2004 Dec;45(12):2361-7. Epub 2004 Sep 16. [PubMed Link Image]
  • Lee BL, New AL, Ong CN: Comparative analysis of conjugated bile acids in human serum using high-performance liquid chromatography and capillary electrophoresis. J Chromatogr B Biomed Sci Appl. 1997 Dec 19;704(1-2):35-42. [PubMed Link Image]
  • Tadano T, Kanoh M, Matsumoto M, Sakamoto K, Kamano T: Studies of serum and feces bile acids determination by gas chromatography-mass spectrometry. Rinsho Byori. 2006 Feb;54(2):103-10. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Bile Acid Biosynthesis SMP00035 Link Image map00120 Link Image
General References
  1. Cowen AE, Korman MG, Hofmann AF, Cass OW, Coffin SB: Metabolism of lithocholate in healthy man. II. Enterohepatic circulation. Gastroenterology. 1975 Jul;69(1):67-76. [PubMed Link Image]
  2. Cowen AE, Korman MG, Hofmann AF, Cass OW: Metabolism of lethocholate in healthy man. I. Biotransformation and biliary excretion of intravenously administered lithocholate, lithocholylglycine, and their sulfates. Gastroenterology. 1975 Jul;69(1):59-66. [PubMed Link Image]
  3. Lee BL, New AL, Ong CN: Comparative analysis of conjugated bile acids in human serum using high-performance liquid chromatography and capillary electrophoresis. J Chromatogr B Biomed Sci Appl. 1997 Dec 19;704(1-2):35-42. [PubMed Link Image]
  4. Cowen AE, Korman MG, Hofmann AF, Thomas PJ: Metabolism of lithocholate in healthy man. III. Plasma disappearance of radioactivity after intravenous injection of labeled lithocholate and its derivatives. Gastroenterology. 1975 Jul;69(1):77-82. [PubMed Link Image]
  5. Tadano T, Kanoh M, Matsumoto M, Sakamoto K, Kamano T: Studies of serum and feces bile acids determination by gas chromatography-mass spectrometry. Rinsho Byori. 2006 Feb;54(2):103-10. [PubMed Link Image]
Metabolic Enzymes
  1. Glycine N-acyltransferase
  2. Glycine N-acyltransferase-like protein 1
  3. Glycine N-acyltransferase-like protein 2
  4. Glycine N-acyltransferase-like protein 3
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
Enzyme 4 [top]
Enzyme 4 ID 12974
Enzyme 4 Name Glycine N-acyltransferase-like protein 3
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name GLYATL3
Enzyme 4 Protein Sequence >Glycine N-acyltransferase-like protein 3
MLVLNCSTKLLILEKMLKSCFPESLKVYGAVMNINRGNPFQKEVVLDSWPDFKAVITRRQ
REAETDNLDHYTNAYAVFYKDVRAYRQLLEECDVFNWDQVFQIQGLQSELYDVSKAVANS
KQLNIKLTSFKAVHFSPVSSLPDTSFLKGPSPRLTYLSVANADLLNRTWSRGGNEQCLRY
IANLISCFPSVCVRDEKGNPVSWSITDQFATMCHGYTLPEHRRKGYSRLVALTLARKLQS
RGFPSQGNVLDDNTASISLLKSLHAEFLPCRFHRLILTPATFSGLPHL
Enzyme 4 Number of Residues 288
Enzyme 4 Molecular Weight 32703.3
Enzyme 4 Theoretical pI 9.04
Enzyme 4 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 4 General Function Involved in glycine N-acyltransferase activity
Enzyme 4 Specific Function Acyltransferase which transfers the acyl group to the N- terminus of glycine
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 222831633 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q5SZD4 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GLYL3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >867 bp
ATGTTGGTGCTAAACTGTTCTACCAAATTACTGATACTGGAGAAAATGTTGAAGAGTTGC
TTTCCTGAATCACTCAAGGTTTACGGAGCGGTGATGAACATAAATCGTGGGAACCCCTTT
CAAAAGGAAGTGGTGTTGGATTCATGGCCGGATTTCAAAGCTGTTATCACCCGACGACAA
AGAGAGGCTGAGACAGATAACCTTGATCATTATACTAATGCCTATGCTGTGTTCTACAAG
GATGTCAGGGCTTATCGACAGCTATTGGAAGAATGTGATGTTTTTAACTGGGACCAAGTT
TTTCAAATACAAGGGCTGCAGAGTGAGTTATATGATGTTTCCAAAGCGGTTGCCAATTCA
AAGCAGTTGAATATAAAGCTAACTTCCTTCAAGGCTGTTCATTTTTCTCCTGTTTCATCT
CTGCCAGATACCAGTTTCCTCAAGGGGCCTTCCCCACGACTAACCTACCTGAGTGTTGCC
AATGCGGATCTACTCAACCGGACTTGGTCCCGGGGAGGCAATGAACAATGTCTCCGGTAC
ATCGCCAACCTCATCTCCTGCTTCCCTAGTGTGTGTGTCCGGGATGAGAAGGGAAACCCG
GTCTCCTGGTCCATCACAGACCAGTTTGCCACCATGTGCCATGGCTACACCCTGCCAGAA
CATCGCAGGAAAGGTTACAGCCGGCTGGTGGCCCTCACGCTGGCCAGGAAGTTGCAAAGC
CGGGGATTCCCCTCTCAGGGGAACGTCCTGGATGACAACACGGCGTCTATAAGCCTCCTG
AAGAGTCTCCATGCTGAGTTCTTGCCTTGTCGCTTCCACAGGCTTATTCTCACCCCTGCG
ACTTTCTCTGGCCTGCCTCACCTCTAG
Enzyme 4 GenBank Gene ID NM_001010904.1 Link Image
Enzyme 4 GeneCard ID GLYATL3 Link Image
Enzyme 4 GenAtlas ID GLYATL3 Link Image
Enzyme 4 HGNC ID HGNC:21349 Link Image
Enzyme 4 Chromosome Location 6
Enzyme 4 Locus 6p12.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available