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Evidence for the involvement of tryptophan 38 in the active site of glutathione S-transferase P.

Abstract：

:Glutathione S-transferase P (GST-P) exists as a homodimeric form and has two tryptophan residues, Trp28 and Trp38, in each subunit. In order to elucidate the role of the two tryptophan residues in catalytic function, we examined intrinsic fluorescence of tryptophan residues and effect of chemical modification by N-bromosuccinimide (NBS). The quenching of intrinsic fluorescence was observed by the addition of S-hexylglutathione, a substrate analogue, and the enzymatic activity was totally lost when single tryptophan residue was oxidized by NBS. To identify which tryptophan residue is involved in the catalytic function, each tryptophan was changed to histidine by site-directed mutagenesis. Trp28His GST-P mutant enzyme showed a comparable enzymatic activity with that of the wild type one. Trp38His mutant neither was bound to S-hexylglutathione-linked Sepharose nor exhibited any GST activity. These findings indicate that Trp38 is important for the catalytic function and substrate binding of GST-P.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Nishihira J,Ishibashi T,Sakai M,Nishi S,Kumazaki T

doi

10.1016/0006-291x(92)91735-9

subject

Has Abstract

pub_date

1992-06-30 00:00:00

pages

1069-77

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(92)91735-9

journal_volume

185

pub_type

杂志文章

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