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.

• PMID: 12646220
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Journal Article | Research Support, Non-U.S. Gov't

Authors

Sahoo R, Sengupta R, Ghosh S

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