当前位置： SCI文献检索 > BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS期刊下所有文献 > Synthesis and initial characterization of gamma-L-glutamyl-L-thiothreonylglycine and gamma-L-glutamyl-L-allo-thiothreonylglycine as steric probes of the active site of glyoxalase I.

Synthesis and initial characterization of gamma-L-glutamyl-L-thiothreonylglycine and gamma-L-glutamyl-L-allo-thiothreonylglycine as steric probes of the active site of glyoxalase I.

Abstract：

:The diastereomeric GSH derivatives gamma-L-Glu-L-allo-thioThr-Gly (6) and gamma-L-Glu-L-thioThr-Gly (6a) have been synthesized as specific probes of the steric environment near the cysteinyl residue of enzyme bound glutathionyl substrates. Experiments with glyoxalase I indicate that while 6a-methylglyoxal thiohemiacetal is a substrate for the enzyme, 6-methylglyoxal thiohemiacetal forms a tight-binding abortive complex with the active site (Ki congruent to 100 microM). Apparently, the small size of the cysteinyl C beta-Hs proton of the normal GSH-methylglyoxal thiohemiacetal substrate for glyoxalase I is a strict requirement for productive substrate binding. These compounds may provide a novel approach to the inhibition of GSH-dependent enzymes.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Xie XF,Creighton DJ

doi

10.1016/0006-291x(91)91975-i

subject

Has Abstract

pub_date

1991-05-31 00:00:00

pages

252-8

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(91)91975-I

journal_volume

177

pub_type

杂志文章

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