Cyclic AMP-independent phosphorylation of Escherichia coli isocitrate dehydrogenase.
The phosphorylation of NADP-specific isocitrate dehydrogenase in a wild-type and in an adenylate cyclase deletion mutant of Escherichia coli has been investigated. The results obtained clearly indicate that cyclic AMP is not required for the phosphorylation reaction per se, not is it for the synthesis or possible activation of the phosphoprotein kinase in this organism. This data are in contrast to results observed in Salmonella typhimurium, and indicate that important differences exist in the phosphorylation of the isocitrate dehydrogenase in these two organisms.
D000085:Acetates / Q000494:pharmacology; D000262:Adenylyl Cyclases / Q000502:physiology; D000242:Cyclic AMP / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D007163:Immunosorbent Techniques; D007521:Isocitrate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007700:Kinetics; D009154:Mutation; D010710:Phosphates / Q000378:metabolism*; D010766:Phosphorylation
D000085:Acetates; D010710:Phosphates; D000242:Cyclic AMP; D007521:Isocitrate Dehydrogenase; D000262:Adenylyl Cyclases