Nitrosative stress on yeast: inhibition of glyoxalase-I and glyceraldehyde-3-phosphate dehydrogenase in the presence of GSNO.
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.
Sahoo
Rupam
R
Department of Biochemistry, University College of Science, Calcutta University, 35, Ballygunge Circular Road, Kolkata 700 019, India.
Sengupta
Rajib
R
Ghosh
Sanjay
S
D000818:Animals; D002474:Cell-Free System; D004791:Enzyme Inhibitors / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007791:Lactoylglutathione Lyase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D020030:Nitric Oxide Donors / Q000378:metabolism*; D012248:Rhodotorula / Q000201:enzymology*; D026422:S-Nitrosoglutathione / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D004791:Enzyme Inhibitors; D020030:Nitric Oxide Donors; D026422:S-Nitrosoglutathione; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D007791:Lactoylglutathione Lyase