In vivo and in vitro studies on the glucose dependent inactivation of yeast cytoplasmic malate dehydrogenase.
The cytoplasmic malate dehydrogenase in the yeast Saccharomyces cerevisiae is known to be inactivated by a glucose dependent process. In this paper it is shown that in vivo effectors of the glucose metabolism (arsenate, iodoacetate, acetaldhyde) inhibit the inactivation or change the inactivation kinetics. In vitro it was possible to inactivate the malate dehydrogenase by addition of the glucose metabolite glyceraldehyde 3-phosphate. The physiological relevance of this modification and the effect of malate dehydrogenase inactivation on the glyoxylate cycle in yeast is discussed.
D000079:Acetaldehyde / Q000494:pharmacology; D001149:Arsenates / Q000494:pharmacology; D002474:Cell-Free System; D003593:Cytoplasm / Q000201:enzymology; D004794:Enzyme Repression / Q000187:drug effects; D005947:Glucose / Q000378:metabolism*; D005994:Glycerophosphates / Q000494:pharmacology; D007461:Iodoacetates / Q000494:pharmacology; D008291:Malate Dehydrogenase / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000378:metabolism
D001149:Arsenates; D005994:Glycerophosphates; D007461:Iodoacetates; D008291:Malate Dehydrogenase; D000079:Acetaldehyde; D005947:Glucose