GLYAT

Glycine-N-acyltransferase, also known as GLYAT, is a human gene.cite web | title = Entrez Gene: GLYAT glycine-N-acyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10249| accessdate = ]

PBB_Summary
section_title =
summary_text = The glycine-N-acyltransferase protein conjugates glycine with acyl-CoA substrates in the mitochondria. The protein is thought to be important in the detoxification of endogenous and xenobiotic acyl-CoA's. Two transcript variants encoding different isoforms have been found for this gene.cite web | title = Entrez Gene: GLYAT glycine-N-acyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10249| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Webster LT, Siddiqui UA, Lucas SV, "et al." |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 |pmid= 931988 |doi=
*cite journal | author=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 | author=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 |doi=
*cite journal | author=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 | author=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=
*cite journal | author=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=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |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
*cite journal | author=SCHACHTER D, TAGGART JV |title=Glycine N-acylase: purification and properties. |journal=J. Biol. Chem. |volume=208 |issue= 1 |pages= 263–75 |year= 2003 |pmid= 13174534 |doi=
*cite journal | author=Suzuki Y, Yamashita R, Shirota M, "et al." |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
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |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

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