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Mitochondrial acyltransferase which transfers an acyl group to the N-terminus of glycine and glutamine, although much less efficiently. Can conjugate numerous substrates to form a variety of N-acylglycines, with a preference for benzoyl-CoA over phenylacetyl-CoA as acyl donors. Thereby detoxify xenobiotics, such as benzoic acid or salicylic acid, and endogenous organic acids, such as isovaleric acid.
Gene References into Functions
GLYAT exhibits mechanistic kinetic cooperativity towards its substrate glycine. PMID: 28759163
Data indicate that Afrikaner caucasians have a Q61L single nucleotide polymorphism (SNP) occurring at a high frequency (12%). PMID: 26149650
SNP variations causing amino acid substitutions in the human GLYAT gene influence the kinetic properties of the enzyme. PMID: 23237781
We identify GLYAT gene which appears to co-regulate bone size phenotypes (BSPs) and appendicular lean mass (ALM). PMID: 23108985
hGLYAT is a good candidate as a novel marker of hepatocellular carcinoma and may be a key molecule in the transition between differentiation and carcinogenesis of liver cells. PMID: 22475485
The aim of this work was to report a comprehensive investigation of GLYAT genetic polymorphisms in DNA samples from 55 subjects of French Caucasian origin. PMID: 20925583
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Subcellular Location
Mitochondrion.
Protein Families
Glycine N-acyltransferase family
Tissue Specificity
Predominantly expressed in liver (at protein level) and kidney. Down-regulated in hepatocellular carcinoma and other liver cancers.