Phosphorylation of isocitrate dehydrogenase in Escherichia coli mutants with a non‐functional glyoxylate cycle

FEBS Letters

Reeves, Henry C.¹  Malloy, Peter J.¹ 

[1] Department of Botany and Microbiology, Arizona State University, Tempe, AZ 85287, USA

关键词: Isocitrate dehydrogenase;    Phosphorylation;    Escherichia coli;    Glyoxylate cycle;    Mutant Phosphoenolpyruvate;    Malate synthase;    Isocitrate lyase;   

DOI  :  10.1016/0014-5793(83)80586-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown