Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
The glycine-N-acyltransferase protein conjugates glycine with acyl-CoA substrates in the mitochondria.
Showing 8 out of 10 products:
GLYAT exhibits mechanistic kinetic cooperativity towards its substrate glycine.
SNP variations causing amino acid substitutions in the human GLYAT gene influence the kinetic properties of the enzyme.
We identify GLYAT gene which appears to co-regulate bone size phenotypes (BSPs) and appendicular lean mass (ALM).
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.
Data suggest a catalytic mechanism for GLYAT in which Glu226 functions to deprotonate glycine, facilitating nucleophilic attack on the benzoyl-CoA; studies involve recombinant protein, molecular modeling, and site-directed mutagenesis.
Mouse glycine N-acyltransferase was successfully overexpressed and purified from Escherichia coli. Benzoyl-CoA and glycine were the substrates with the highest (kcat/Km)app (show APP Proteins) values.
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.
, acyl-CoA:glycine N-acyltransferase
, aralkyl acyl-CoA N-acyltransferase
, aralkyl acyl-CoA:amino acid N-acyltransferase
, aralkyl-CoA N-acyltransferase
, benzoyl-coenzyme A:glycine N-acyltransferase
, glycine N-acyltransferase
, glycine N-benzoyltransferase
, liver regeneration-related protein LRRG067