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Phosphorylation of isocitrate lyase in Escherichia coli



Phosphorylation of isocitrate lyase in Escherichia coli



Biochimie 71(9-10): 1065-1070



Isocitrate lyase from Escherichia coli becomes phosphorylated in vitro by an endogenous kinase when partially purified extracts are incubated with [gamma-32P]ATP. Treatment of isocitrate lyase with histidine modifying reagents, and alkaline hydrolysis of in vitro phosphorylated enzyme indicated the presence of a phosphohistidine residue. Phosphorylation of isocitrate lyase can also occur in vivo, which indicates a possible regulatory significance of this modification. In addition to phosphorylation, isocitrate lyase is capable of incorporating label from both [alpha-32P]ATP and [14C]ATP suggesting that more than one type of covalent modification occurs on this enzyme. This report reviews the studies which have demonstrated the phosphorylation and modification of isocitrate lyase from Escherichia coli.

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Accession: 040970967

Download citation: RISBibTeXText

PMID: 2512997

DOI: 10.1016/0300-9084(89)90112-0


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