GLYAT

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.

The literature reports it to be approximately 30 kDa, or approximately 27 kDa.{{cite journal |vauthors=van der Westhuizen FH, Pretorius PJ, Erasmus E | title = The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase | journal = J. Biochem. Mol. Toxicol. | volume = 14 | issue = 2 | pages = 102–9 | year = 2000 | pmid = 10630424 | doi = 10.1002/(SICI)1099-0461(2000)14:2<102::AID-JBT6>3.0.CO;2-H | s2cid = 44672034 }} 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{{cite journal | vauthors = Nandi DL, Lucas SV, Webster LT | title = Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization | journal = J. Biol. Chem. | volume = 254 | issue = 15 | pages = 7230–7 | date = August 1979 | doi = 10.1016/S0021-9258(18)50309-4 | pmid = 457678 | doi-access = free }}{{cite journal |vauthors=Kelley M, Vessey DA | title = Structural comparison between the mitochondrial aralkyl-CoA and arylacetyl-CoA N-acyltransferases | journal = Biochem. J. | volume = 288 | issue = 1| pages = 315–7 |date=November 1992 | pmid = 1445276 | pmc = 1132116 | doi = 10.1042/bj2880315}}

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• {{cite journal |vauthors=Webster LT, Siddiqui UA, Lucas SV |title=Identification of separate acyl- CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man. |journal=J. Biol. Chem. |volume=251 |issue= 11 |pages= 3352–8 |year= 1976 |doi=10.1016/S0021-9258(17)33444-0 |pmid= 931988 |display-authors=etal|doi-access=free }}
• {{cite journal |vauthors=Mawal YR, Qureshi IA |title=Purification to homogeneity of mitochondrial acyl coa:glycine n-acyltransferase from human liver. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 2 |pages= 1373–9 |year= 1994 |pmid= 7802672 |doi= 10.1006/bbrc.1994.2817 }}
• {{cite journal |vauthors=Mawal YR, Qureshi IA |title=An immunodetection method for the quantitation of human acyl CoA:glycine N-acyltransferase in biological samples. |journal=Biochem. Mol. Biol. Int. |volume=34 |issue= 3 |pages= 595–601 |year= 1995 |pmid= 7833837 }}
• {{cite journal |vauthors=Merkler DJ, Merkler KA, Stern W, Fleming FF |title=Fatty acid amide biosynthesis: a possible new role for peptidylglycine alpha-amidating enzyme and acyl-coenzyme A: glycine N-acyltransferase. |journal=Arch. Biochem. Biophys. |volume=330 |issue= 2 |pages= 430–4 |year= 1996 |pmid= 8660675 |doi= 10.1006/abbi.1996.0272 }}
• {{cite journal |vauthors=Mawal Y, Paradis K, Qureshi IA |title=Developmental profile of mitochondrial glycine N-acyltransferase in human liver. |journal=J. Pediatr. |volume=130 |issue= 6 |pages= 1003–7 |year= 1997 |pmid= 9202629 |doi=10.1016/S0022-3476(97)70293-2 }}
• {{cite journal |vauthors=van der Westhuizen FH, Pretorius PJ, Erasmus E |title=The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase. |journal=J. Biochem. Mol. Toxicol. |volume=14 |issue= 2 |pages= 102–9 |year= 2000 |pmid= 10630424 |doi=10.1002/(SICI)1099-0461(2000)14:2<102::AID-JBT6>3.0.CO;2-H |s2cid=44672034 }}
• {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
• {{cite journal |vauthors=SCHACHTER D, TAGGART JV |title=Glycine N-acylase: purification and properties. |journal=J. Biol. Chem. |volume=208 |issue= 1 |pages= 263–75 |year= 2003 |doi=10.1016/S0021-9258(18)65643-1 |pmid= 13174534 |doi-access=free }}
• {{cite journal |vauthors=Suzuki Y, Yamashita R, Shirota M |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711–8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604 | pmc=515316 |display-authors=etal}}
• {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}

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• {{UCSC genome browser|GLYAT}}
• {{UCSC gene details|GLYAT}}

{{Gene-11-stub}}