- P-ISSN 1225-0163
- E-ISSN 2288-8985
- P-ISSN1225-0163
- E-ISSN2288-8985
- SCOPUS, ESCI, KCI
Article Detail
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Functional analysis of Tyr7 residue in human glutathione S-transferase P1-1
Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985
1997, v.10 no.5, pp.378-385
Kong,
K., Park,
H., Yoon,
S., &
Cho,
S.
(1997). Functional analysis of Tyr7 residue in human glutathione S-transferase P1-1. Analytical Science and Technology, 10(5), 378-385.
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Abstract
In order to clarify the functional role of Tyr7 in human glutathione S-transferase P1-1, we extensively investigated the effect of mutation of Tyr7 on the substrate specificity and inhibition characteristics. The mutational replacement of Tyr7 with phenylalanine lowered the specific activities with 1,2-dichloro-4-nitrobenzene and 1,2-epoxy-3-(p-nitrophenoxy) propane for GSH-conjugation reaction to 3~5% of the values for the wild-type enzyme. The pKa of the thiol group of GSH bound in Y7F was about 2.4 pK units higher than that in the wild-type enzyme. The <TEX>$I_{50}$</TEX> of hematin for Y7F was similar to that for the wild-type enzyme and those of benastatin A and S-(2,4-dinitrophenyl)glutathione were only moderately decreased. These results suggest that Tyr7 is considered to be important the catalytic activities not only for GSH-chloronitrobenzene derivatives but also for GSH-epoxide conjugation reaction, rather than to binding of the substrates.
- keywords
- glutathione S-tranferase, tyrosine 7 residue, active site, substrate spedficity, inhibition characteristics
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