GLYAT

Glycine-N-acyltransferase, also known as GLYAT, is an enzyme which in humans is encoded by the GLYAT gene.

GLYAT
Identifiers
Aliases	GLYAT, ACGNAT, CAT, GAT, glycine-N-acyltransferase
External IDs	OMIM: 607424; MGI: 2147502; HomoloGene: 64840; GeneCards: GLYAT; OMA:GLYAT - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q12.1 Start 58,640,426 bp End 58,731,974 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19|19 A Start 12,610,672 bp End 12,631,275 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver kidney tubule glomerulus metanephric glomerulus renal medulla subcutaneous adipose tissue sural nerve abdominal fat tibialis anterior muscle human kidney Top expressed in right kidney human kidney left lobe of liver proximal tubule lumbar spinal ganglion facial motor nucleus lumbar subsegment of spinal cord anterior horn of spinal cord primary visual cortex crypt of lieberkuhn of small intestine More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity acyltransferase activity protein binding glycine N-acyltransferase activity glycine N-benzoyltransferase activity Cellular component mitochondrial matrix mitochondrion Biological process xenobiotic metabolic process acyl-CoA metabolic process monocarboxylic acid metabolic process response to toxic substance glycine metabolic process benzoyl-CoA metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10249 107146 Ensembl ENSG00000149124 ENSMUSG00000063683 UniProt Q6IB77 Q91XE0 RefSeq (mRNA) NM_201648 NM_005838 NM_145935 RefSeq (protein) NP_005829 NP_964011 NP_666047 Location (UCSC) Chr 11: 58.64 – 58.73 Mb Chr 19: 12.61 – 12.63 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

The glycine-N-acyltransferase protein conjugates glycine with acyl-CoA substrates in the mitochondria primarily in liver and kidney. The glycine N-acyltransferase enzyme is involved in the detoxification of a wide range of xenobiotic and endogenous metabolites. These include benzoic acid, a compound found in fruits and vegetables and used in medicine and foodstuffs as a preservative; salicylic acid, a metabolite of aspirin; and several endogenous metabolites. The diversity is demonstrated by the wide range of acylglycines excreted in the urines of patients with defects of organic acid metabolism. No defect of glycine N-acyltransferase has yet been described, but it has been demonstrated that there is significant inter individual variation in glycine conjugation capacity. Human glycine N-acyltransferase isoform a is a 296 amino acid protein translated from mRNA transcript splice variant 1. It is encoded by exons 2 to 6 of the mRNA transcript.

Molecular weight

The literature reports it to be approximately 30 kDa, or approximately 27 kDa. The predicted size is 33.9 KDa. For the bovine enzyme a range of sizes between approximately 33 kDa and about 36 KDa is reported (Nandi, 1979, Vessey, 1992, van der Westhuizen, 2000). The predicted size of bovine GLYAT based on its sequence (accession number nm: 177486), is 33.9 kDa. This compares well to the experimentally determined sizes

Further reading

• Webster LT, Siddiqui UA, Lucas SV, et al. (1976). "Identification of separate acyl- CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man". J. Biol. Chem. 251 (11): 3352–8. doi:10.1016/S0021-9258(17)33444-0. PMID 931988.
• Mawal YR, Qureshi IA (1994). "Purification to homogeneity of mitochondrial acyl coa:glycine n-acyltransferase from human liver". Biochem. Biophys. Res. Commun. 205 (2): 1373–9. doi:10.1006/bbrc.1994.2817. PMID 7802672.
• Mawal YR, Qureshi IA (1995). "An immunodetection method for the quantitation of human acyl CoA:glycine N-acyltransferase in biological samples". Biochem. Mol. Biol. Int. 34 (3): 595–601. PMID 7833837.
• Merkler DJ, Merkler KA, Stern W, Fleming FF (1996). "Fatty acid amide biosynthesis: a possible new role for peptidylglycine alpha-amidating enzyme and acyl-coenzyme A: glycine N-acyltransferase". Arch. Biochem. Biophys. 330 (2): 430–4. doi:10.1006/abbi.1996.0272. PMID 8660675.
• Mawal Y, Paradis K, Qureshi IA (1997). "Developmental profile of mitochondrial glycine N-acyltransferase in human liver". J. Pediatr. 130 (6): 1003–7. doi:10.1016/S0022-3476(97)70293-2. PMID 9202629.
• van der Westhuizen FH, Pretorius PJ, Erasmus E (2000). "The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase". J. Biochem. Mol. Toxicol. 14 (2): 102–9. doi:10.1002/(SICI)1099-0461(2000)14:2<102::AID-JBT6>3.0.CO;2-H. PMID 10630424. S2CID 44672034.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• SCHACHTER D, TAGGART JV (2003). "Glycine N-acylase: purification and properties". J. Biol. Chem. 208 (1): 263–75. doi:10.1016/S0021-9258(18)65643-1. PMID 13174534.
• Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

External links

• GLYAT human gene location in the UCSC Genome Browser.
• GLYAT human gene details in the UCSC Genome Browser.