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Phosphorylation of isocitrate dehydrogenase in Escherichia coli mutants with a non‐functional glyoxylate cycle
Author(s) -
Reeves Henry C.,
Malloy Peter J.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80586-9
Subject(s) - glyoxylate cycle , isocitrate dehydrogenase , malate synthase , isocitrate lyase , biochemistry , citric acid cycle , malate dehydrogenase , escherichia coli , idh1 , phosphoenolpyruvate carboxykinase , phosphorylation , dehydrogenase , biology , enzyme , chemistry , mutant , gene
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.