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Multiplicity of phosphorylation sites onEscherichia coli isocitrate dehydrogenase

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Abstract

Several lines of evidence indicate that the in vivo phosphorylation of isocitrate dehydrogenase (EC 1.1.1.42) inEscherichia coli occurs at multiple sites: first, the phosphorylated enzyme can be resolved by two-dimensional electrophoresis into three distinct spots differing in charge; second, the analysis of its phosphoamino acid content shows that it is modified at both serine and threonine residues; third, its extensive hydrolysis by proteolytic enzymes yields several different phosphopeptides.

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Authors and Affiliations

  1. Laboratory of Molecular Biology, University of Lyon, Villeurbanne, France

    Jean-Claude Cortay

  2. Department of Botany and Microbiology, Arizona State University, 85287, Tempe, Arizona, USA

    Henry C. Reeves

Authors
  1. Jean-Claude Cortay
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  2. Henry C. Reeves
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  3. Alain J. Cozzone
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Cortay, JC., Reeves, H.C. & Cozzone, A.J. Multiplicity of phosphorylation sites onEscherichia coli isocitrate dehydrogenase. Current Microbiology 13, 251–254 (1986). https://doi.org/10.1007/BF01568648

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  • DOI: https://doi.org/10.1007/BF01568648

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