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SetFSB - 03/21/2009 Added ICS9LPRS477BKL(Asus M3A). Supported AMD-790GX chipset. - 03/20/2009 Added CV193CPAG(ECS X58B-A), CY28349BOC(HP .NAD+-dependent reduction of arylacetamide deacetylase by a novel glutathione S-transferase. The purpose of this study was to purify a novel arylacetamide deacetylase that is present in arylacetamide-treated rat liver cytosol. With rat liver cytosol, arylacetamides were found to be efficient substrates of the deacetylase. The enzyme activity was induced by the administration of 3-methylcholanthrene to rats. Sephadex G-150 gel chromatography revealed that the enzyme activity was associated with a protein of Mr around 33 kDa, which is slightly smaller than the molecular size of glutathione S-transferase Yb1 and S4. The enzyme activity was specific for arylacetamides and deacetylated N-(4-hydroxyphenyl)acetamide, N-(4-hydroxyphenyl)succinamide, N-(4-hydroxyphenyl)acetoamide and N-(4-hydroxyphenyl)aziridinium. Arylacetamides also served as inhibitors of the enzyme activity. Aldehyde formation was not detected during the arylacetamide deacetylation reaction. The deacetylase required NADH and NADPH. It was specific for NAD+, with no activity in the presence of NADH or NADPH. A chemically synthesized arylacetamide deacetylase-NAD+ complex was found to have a stoichiometry of 1 mol of enzyme subunit to 1 mol of NAD+. Studies with peptide mapping using CNBr cleavage revealed that the active site of the deacetylase was located at the N-terminal region, which corresponded to a glutathione-binding site of glutathione S-transferase. Furthermore, we determined that the deacetylase required GSH and glutathione S-transferase Yb1 and S4 in the reaction system. These results indicate that arylacetamide deacet

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