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.
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container_title Science (American Association for the Advancement of Science)
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creator Garnak, Margit
Reeves, Henry C.
description 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.
doi_str_mv 10.1126/science.34215
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subjects 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
title Phosphorylation of Isocitrate Dehydrogenase of Escherichia coli
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