Phosphorylation of isocitrate dehydrogenase in Escherichia coli mutants with a non-functional glyoxylate cycle.
The phosphorylation of NADP-specific isocitrate dehydrogenase in an isocitrate lyase and in a malate synthase mutant of Escherichia coli has been investigated. The results clearly demonstrate that isocitrate dehydrogenase may undergo an acetate-induced phosphorylation in organisms which do not have a functional glyoxylate cycle. This observation, together with those reported in Salmonella typhimurium, suggest that the current notion concerning the interrelationship between the glyoxylate cycle and the reversible phosphorylation of NADP-isocitrate dehydrogenase in microbial physiology should be reevaluated, and that phosphoenolpyruvate may be a key factor in the regulation of the reversible covalent modification of this enzyme in vivo.
D001426:Bacterial Proteins / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006038:Glyoxylates / Q000378:metabolism*; D007521:Isocitrate Dehydrogenase / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D010766:Phosphorylation
D001426:Bacterial Proteins; D006038:Glyoxylates; D007521:Isocitrate Dehydrogenase