BMB Reports
- 제31권4호
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- Pages.399-404
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- 1998
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- 1976-670X(eISSN)
Active-Site Mutants of Human Glutathione S-Transferase P1-1: Effects of the Mutations on Substrate Specificity and Inhibition Characteristics
- Park, Hee-Joong (Department of Chemistry, College of Natural Sciences, Chung-Ang University) ;
- Yoon, Suck-Young (Department of Chemistry, College of Natural Sciences, Chung-Ang University) ;
- Kong, Kwang-Hoon (Department of Chemistry, College of Natural Sciences, Chung-Ang University)
- 투고 : 1998.04.15
- 발행 : 1998.07.31
초록
In order to gain further insight on the relationship between structure and function of glutathione S-transferase (GST), the six active-site mutants, R13T, K44T, Q51A, Q64A, S65A, and D98A, of human GST P1-1 were expressed in Escherichia coli and purified to electrophoretic homogeneity by affinity chromatography on immobilized GSH. The active-site mutants showed marked differences in substrate specificity. The substitution of Gln51 with threonine resulted in a drastic decrease in the specific activities to <10% of the wild-type value. The substitution of Arg13 with threonine resulted in more decreased specific activity toward cumene hydroperoxide and in the
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