Nitrosative stress on yeast: inhibition of glyoxalase-I and glyceraldehyde-3-phosphate dehydrogenase in the presence of GSNO.

Abstract:

:Under nitrosative stressed condition intracellular GSNO accumulation is common to all cell types. Conserved NADH-dependent GSNO reductase was reported previously as an important cellular protective measure against this. In spite of the constitutive nature of the enzyme, we observed in vivo inactivation of two important enzymes-glyoxalase-I and glyceraldehyde-3-phosphate dehydrogenase under 5 mM GSNO stress in two budding yeasts, though with difference in their sensitivity. Former was more susceptible to inactivation in in vitro condition, too. In this study, we explored the competitive nature of yeast glyoxalase-I inhibition by GSNO. GSNO actually competes with GSH substrate-binding site of the enzyme.

authors

Sahoo R,Sengupta R,Ghosh S

doi

10.1016/s0006-291x(03)00251-1

subject

Has Abstract

pub_date

2003-03-21 00:00:00

pages

665-70

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006291X03002511

journal_volume

302

pub_type

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