Kitada M, McLenithan J C, Anders M W
J Biol Chem. 1985 Sep 25;260(21):11749-54.
An enzyme catalyzing the reduction of S-(2,4-dichlorophenacyl)glutathione to 2',4'-dichloroacetophenone was purified to apparent homogeneity by ion exchange, gel filtration, and hydroxylapatite chromatography from rat hepatic cytosol. The molecular weight was 30,000-37,000. The enzyme is distinct from the glutathione S-transferases, mercaptopyruvate sulfurtransferase, and glyoxalase I. Substrate specificity studies showed that S-phenacylglutathiones are the preferred first substrates and that several thiols (glutathione, mercaptoethanol, L-cysteine, or cysteamine) serve as reducing substrates. The enzyme serves to convert toxic alpha-haloketones, which react rapidly and nonenzymatically with glutathione, to nontoxic alkyl ketones.
一种催化S-(2,4-二氯苯甲酰基)谷胱甘肽还原为2',4'-二氯苯乙酮的酶，通过离子交换、凝胶过滤和羟基磷灰石层析从大鼠肝细胞溶胶中纯化至表观均一。分子量为30,000 - 37,000。该酶与谷胱甘肽S-转移酶、巯基丙酮酸硫转移酶和乙二醛酶I不同。底物特异性研究表明，S-苯甲酰基谷胱甘肽是首选的第一底物，几种硫醇（谷胱甘肽、巯基乙醇、L-半胱氨酸或半胱胺）作为还原底物。该酶用于将与谷胱甘肽快速非酶反应的有毒α-卤代酮转化为无毒的烷基酮。
