Phosphorylation of Isocitrate Dehydrogenase of Escherichia coli

Addition of acetate to a stationary phase culture of Escherichia coli in glycerol mineral salts medium containing phosphorus-32-labeled orthophosphate results in rapid loss of isocitrate dehydrogenase activity and concomitant incorporation of phosphorus-32 into the enzyme. This is the first example...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1979-03, Vol.203 (4385), p.1111-1112
Hauptverfasser:	Garnak, Margit, Reeves, Henry C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetates Acetates - metabolism Bacteria Citrates Dehydrogenases Enzymes Escherichia coli - enzymology Gels Isocitrate Dehydrogenase - metabolism Isocitrates NADP - metabolism Phosphorylation Protein Kinases - metabolism Radioactive decay Serine - metabolism Sodium Threonine - metabolism
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Zusammenfassung:	Addition of acetate to a stationary phase culture of Escherichia coli in glycerol mineral salts medium containing phosphorus-32-labeled orthophosphate results in rapid loss of isocitrate dehydrogenase activity and concomitant incorporation of phosphorus-32 into the enzyme. This is the first example of protein phosphorylation in a bacterium in which the endogenous substrate for the protein kinase has been identified.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.34215