GLYAT

From Wikipedia, the free encyclopedia

Glycine-N-acyltransferase

Identifiers

GLYAT; CAT; ACGNAT; GAT

External IDs

OMIM: 607424 MGI: 2147502 HomoloGene: 64840

Gene ontology
Molecular Function:	• acyltransferase activity • transferase activity • glycine N-acyltransferase activity
Cellular Component:	• mitochondrion
Biological Process:	• acyl-CoA metabolic process • response to toxin

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005838 (mRNA)
NP_005829 (protein)

NM_145935 (mRNA)
NP_666047 (protein)

Location

Chr 11: 58.23 - 58.26 Mb

Chr 19: 12.7 - 12.72 Mb

Pubmed search

[1]

[2]

Glycine-N-acyltransferase, also known as GLYAT, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: GLYAT glycine-N-acyltransferase.

[edit] 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. PMID 931988.
Mawal YR, Qureshi IA (1995). "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. 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. PMID 10630424.
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. doi:10.1073/pnas.242603899. PMID 12477932.
SCHACHTER D, TAGGART JV (2003). "Glycine N-acylase: purification and properties.". J. Biol. Chem. 208 (1): 263–75. 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. 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. PMID 15489334.