Alternative titles; symbols
HGNC Approved Gene Symbol: GLYAT
Cytogenetic location: 11q12.1 Genomic coordinates (GRCh38): 11:58,708,757-58,731,943 (from NCBI)
Many carboxylic acid xenobiotics are conjugated with an amino acid, primarily glycine, before excretion. The conjugation involves a 2-step pathway initiated by the activation of the carboxylic acid to the coenzyme A thioester by butyrate:CoA ligase. GLYAT (EC 2.3.1.65) then transfers the acyl group to the N terminal of glycine.
Matsuo et al. (2012) cloned full-length GLYAT by PCR and RACE of a human liver cDNA library. The deduced protein contains 295 amino acids. Northern blot analysis detected a 1.2-kb transcript. Quantitative RT-PCR detected highest GLYAT expression in liver and kidney. Immunohistochemical analysis and cell fractionation of transfected HeLa cells revealed mitochondrial localization.
Mawal and Qureshi (1994) characterized GLYAT, which they called ACGNAT, purified from human liver. The monomeric enzyme had an apparent molecular mass of 30 kD, and it showed activity against benzoyl-CoA, salicyl-CoA, isovaleryl-CoA, and octanoyl-CoA.
Mawal et al. (1997) examined the developmental profile of ACGNAT in human liver. They determined that the activity of ACGNAT increases until age 18 months, when it reaches adult levels, and remains constant until age 40 years.
Using benzoyl- and phenylacetyl-CoA as acyl donors and glycine and glutamine as acyl acceptors, Matsuo et al. (2012) found that purified recombinant human GLYAT effectively catalyzed transfer of benzoyl to glycine. GLYAT mRNA and protein expression was significantly downregulated in several types of liver cancers compared with normal tissue. GLYAT was not downregulated in hepatitis of any etiology.
By genomic sequence analysis, Zhang et al. (2007) mapped the GLYAT gene to an approximately 300-kb region of chromosome 11q12.1 that also contains GLYATL1 (614761) and GLYATL2 (614762).
Matsuo, M., Terai, K., Kameda, N., Matsumoto, A., Kurokawa, Y., Funase, Y., Nishikawa, K., Sugaya, N., Hiruta, N., Kishimoto, T. Designation of enzyme activity of glycine-N-acyltransferase family genes and depression of glycine-N-acyltransferase in human hepatocellular carcinoma. Biochem. Biophys. Res. Commun. 420: 901-906, 2012. [PubMed: 22475485] [Full Text: https://doi.org/10.1016/j.bbrc.2012.03.099]
Mawal, Y., Paradis, K., Qureshi, I. A. Developmental profile of mitochondrial glycine N-acyltransferase in human liver. J. Pediat. 130: 1003-1007, 1997. [PubMed: 9202629] [Full Text: https://doi.org/10.1016/s0022-3476(97)70293-2]
Mawal, Y. R., Qureshi, I. A. Purification to homogeneity of mitochondrial acyl CoA:glycine N-acyltransferase from human liver. Biochem. Biophys. Res. Commun. 205: 1373-1379, 1994. [PubMed: 7802672] [Full Text: https://doi.org/10.1006/bbrc.1994.2817]
Zhang, H., Lang, Q., Li, J., Zhong, Z., Xie, F., Ye, G., Wan, B., Yu, L. Molecular cloning and characterization of a novel human glycine-N-acyltransferase gene GLYATL1, which activates transcriptional activity of HSE pathway. Int. J. Molec. Sci. 8: 433-444, 2007.