The specificity of glycine-N-acylase and acylglycine excretion in the organicacidaemias
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Cited by (85)
The glycine N-acyltransferases, GLYAT and GLYATL1, contribute to the detoxification of isovaleryl-CoA - an in-silico and in vitro validation
2023, Computational and Structural Biotechnology JournalEnzymology of Amino Acid Conjugation Reactions
2018, Comprehensive Toxicology: Third EditionConservation of the coding regions of the glycine N-acyltransferase gene further suggests that glycine conjugation is an essential detoxification pathway
2015, GeneCitation Excerpt :Recently interest in glycine conjugation has increased, due to the emerging clinical relevance of glycine conjugation, after research in this field had been neglected for several decades (Badenhorst et al., 2013, 2014; Lees et al., 2013; Beyoglu and Idle, 2012). Glycine N-acyltransferase (GLYAT, EC 2.3.1.13) is responsible for the glycine conjugation of xenobiotics (Nandi et al., 1979; Schachter and Taggart, 1954; Tanaka and Isselbacher, 1967) such as benzoic acid, salicylic acid and several endogenous metabolites such as isovaleric acid (Bartlett and Gompertz, 1974; Campbell et al., 1988). Xenobiotics that undergo glycine conjugation are activated to an acyl-CoA by the mitochondrial medium chain acid:CoA ligases (Killinberg et al., 1971; Knights, 1998).
Expression, purification, and characterization of mouse glycine N-acyltransferase in Escherichia coli
2014, Protein Expression and PurificationCitation Excerpt :Amino acceptor substrate preference ranked in decreasing order is benzoyl-CoA > butyryl-CoA > hexanoyl-CoA > acetyl-CoA under these standard conditions of this study. These data are consistent with earlier reports for mammalian GLYATs purified from natural sources [8,9,11–14,30–34]. The activity data of Table 1 combined with the data included in Fig. 2 demonstrate that we have successfully expressed and purified active, recombinant mGLYAT from E. coli.
Characterisation of the influence of genetic variations on the enzyme activity of a recombinant human glycine N-acyltransferase
2013, GeneCitation Excerpt :It is not known at present whether known non-synonymous variations in the GLYAT gene may account for some of this variability (Lino Cardenas et al., 2010; Yamamoto et al., 2009). The enzymatic characteristics of GLYAT have been studied using enzymes isolated from the liver and kidney of several mammals (Bartlett and Gompertz, 1974; Gregersen et al., 1986; Kelley and Vessey, 1993, 1994; Kolvraa and Gregersen, 1986; Mawal and Qureshi, 1994). The values reported for the molecular mass, apparent Michaelis constant (KMapp), and maximum velocity of human liver GLYAT, are highly variable (Table 1).