Glutathione reductase directly mediates the stimulation of yeast glucose-6-phosphate dehydrogenase by GSSG.
Yeast glucose-6-phosphate dehydrogenase was inhibited by low NADPH concentrations in cell-free extracts, and de-inhibited by GSSG; extensive dialysis of the crude extract did not diminish the GSSG effect. Immunoprecipitation of glutathione reductase abolished the de-inhibition of glucose-6-phosphate dehydrogenase by GSSG. Purified glucose-6-phosphate dehydrogenase was inhibited by NADPH but not de-inhibited by GSSG, and upon addition of pure glutathione reductase GSSG completely de-inhibited the glucose-6-phosphate dehydrogenase.
Llobell
A
A
Departamento de Bioquímica y Biología Molecular (Veterinaria), Universidad de Córdoba, Spain.
Lopez-Ruiz
A
A
Peinado
J
J
Lopez-Barea
J
J
D000906:Antibodies; D004789:Enzyme Activation / Q000187:drug effects; D005954:Glucosephosphate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D005978:Glutathione / Q000031:analogs & derivatives* / Q000494:pharmacology; D019803:Glutathione Disulfide; D005980:Glutathione Reductase / Q000276:immunology / Q000494:pharmacology*; D009249:NADP / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D000906:Antibodies; D009249:NADP; D005954:Glucosephosphate Dehydrogenase; D005980:Glutathione Reductase; D005978:Glutathione; D019803:Glutathione Disulfide