Sexton D J, Dimmock J R, Mutus B
Department of Chemistry and Biochemistry, University of Windsor, Ont., Canada.
Biochem Cell Biol. 1993 Jan-Feb;71(1-2):98-101. doi: 10.1139/o93-016.
The conjugation of 1-p-chlorophenyl-4,4-dimethyl-5-diethylamino-1-penten-3- one hydrobromide (CDDP), a Mannich base of an alpha,beta-unsaturated ketone, to glutathione is catalyzed selectively by alpha-class glutathione S-transferase. The reaction of CDDP with glutathione can be monitored continuously by following the conjugation-dependent decrease in absorbance of CDDP at 307 nm. The Km and Vmax for CDDP with alpha-class glutathione S-transferase from horse liver were determined to be 226 microM and 14.6 mumol/(min.mg), respectively. CDDP is the first example of an alpha-class glutathione S-transferase selective substrate that monitors the glutathione conjugation activity, rather than the glutathione peroxidase activity of the enzyme.
α-类谷胱甘肽S-转移酶可选择性催化α,β-不饱和酮的曼尼希碱1-对氯苯基-4,4-二甲基-5-二乙氨基-1-戊烯-3-酮氢溴酸盐（CDDP）与谷胱甘肽的结合反应。通过跟踪CDDP在307 nm处吸光度的结合依赖性降低，可以连续监测CDDP与谷胱甘肽的反应。马肝α-类谷胱甘肽S-转移酶催化CDDP反应的Km和Vmax分别测定为226 μM和14.6 μmol/（min·mg）。CDDP是首个用于监测谷胱甘肽结合活性而非该酶谷胱甘肽过氧化物酶活性的α-类谷胱甘肽S-转移酶选择性底物实例。
