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Science 16 March 1979:
Vol. 203. no. 4385, pp. 1111 - 1112
DOI: 10.1126/science.34215
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Articles

Science, Vol 203, Issue 4385, 1111-1112
Copyright © 1979 by American Association for the Advancement of Science

articles

Phosphorylation of Isocitrate dehydrogenase of Escherichia coli

M Garnak and HC Reeves

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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria.
J. Deutscher, C. Francke, and P. W. Postma (2006)
Microbiol. Mol. Biol. Rev. 70, 939-1031
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Posttranslational Protein Modification in Archaea.
J. Eichler and M. W. W. Adams (2005)
Microbiol. Mol. Biol. Rev. 69, 393-425
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The Acetate Switch.
A. J. Wolfe (2005)
Microbiol. Mol. Biol. Rev. 69, 12-50
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Bacillus subtilis Isocitrate Dehydrogenase. A SUBSTRATE ANALOGUE FOR ESCHERICHIA COLI ISOCITRATE DEHYDROGENASE KINASE/PHOSPHATASE.
S. K. Singh, S. P. Miller, A. Dean, L. J. Banaszak, and D. C. LaPorte (2002)
J. Biol. Chem. 277, 7567-7573
   Abstract »    Full Text »    PDF »
Quantitative Determination of Metabolic Fluxes during Coutilization of Two Carbon Sources: Comparative Analyses with Corynebacterium glutamicum during Growth on Acetate and/or Glucose.
V. F. Wendisch, A. A. de Graaf, H. Sahm, and B. J. Eikmanns (2000)
J. Bacteriol. 182, 3088-3096
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Locations of the Regulatory Sites for Isocitrate Dehydrogenase Kinase/Phosphatase.
S. P. Miller, R. Chen, E. J. Karschnia, C. Romfo, A. Dean, and D. C. LaPorte (2000)
J. Biol. Chem. 275, 833-839
   Abstract »    Full Text »    PDF »
Isocitrate Dehydrogenase Kinase/Phosphatase. KINETIC CHARACTERISTICS OF THE WILD-TYPE AND TWO MUTANT PROTEINS.
S. P. Miller, E. J. Karschnia, T. P. Ikeda, and D. C. LaPorte (1996)
J. Biol. Chem. 271, 19124-19128
   Abstract »    Full Text »    PDF »
Active Site Phosphorylation of Enzyme I of the Bacterial Phosphotransferase System by an ATP-dependent Kinase.
H. K. Dannelly and S. Roseman (1996)
J. Biol. Chem. 271, 15285-15291
   Abstract »    Full Text »    PDF »
Transmission of Regulatory Conformational Changes through Proteins.
P.E. Thorsness, S.L. Mowbray, and D.E. Koshland Jr. (1987)
Cold Spring Harb Symp Quant Biol 52, 623-630
   Abstract »    PDF »


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