Abstract
The glycine-N-acyltransferase (GLYAT) is well known to be involved in thedetoxification of endogenous and exogenous xenobiotic acyl-CoA's in mammals.Unfortunately, the knowledge about the gene encoding GLYAT is very limited. Here wereport a novel gene encoding a GLYAT member, designated as GLYATL1, which was1546 base pairs in length and contained an open reading frame (ORF) encoding apolypeptide of 302 amino acids. GLYATL1 was a split gene that was consisted of 7 exonsand 6 introns and mapped to chromosome 11q12.1. The expression of GLYATL1 could befound in liver, kidney, pancreas, testis, ovary and stomach among 18 human tissues by RT-PCR analysis. Subcellular localization of myc-tagged GLYATL1 fusion protein revealedthat GLYATL1 was distributed primarily in the cytoplasm of COS-7 cells. Furthermore,through the pathway profiling assay, the GLYATL1 protein was found to activate HSEsignaling pathway in a dose-dependent manner when overexpressed in HEK293T cells.
Highlights
The GLYATs (EC 2.3.1.13) present a family of proteins which play a physiologically important role in the detoxification of endogenous and xenobiotic acyl-CoA's
The conjugation, which occurs in both liver and kidney [1], involves in a two step pathway: firstly, the carboxylic acid is ATP-dependent activated with CoA by carboxylic acid: CoA ligase to form an intermediate acyl-CoA product Gatley [1,2,3]; this acyl group is transferred to the amino group of glycine by the action of an Glycine- N-acyltransferase(GLYAT)
The results showed that GLYATL1 was a cytoplasm protein when overexpressed in the COS-7 cells
Summary
The GLYATs (EC 2.3.1.13) present a family of proteins which play a physiologically important role in the detoxification of endogenous and xenobiotic acyl-CoA's. A variety of carboxylic acids xenobioties were conjugated with an amino acid, primarily glycine [1], and the resulting peptides appear as excretory products in the urine. The conjugation, which occurs in both liver and kidney [1], involves in a two step pathway: firstly, the carboxylic acid is ATP-dependent activated with CoA by carboxylic acid: CoA ligase to form an intermediate acyl-CoA product Gatley [1,2,3]; this acyl group is transferred to the amino group of glycine by the action of an Glycine- N-acyltransferase(GLYAT). It is clearly demonstrated that the enzyme has two kind of substrates in its functional pathway: the acyl-CoA donor and acyl-acceptor. The acyl-CoA acceptor exhibits relatively high specifity for glycine [1,7]
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