Phosphorylation of isocitrate dehydrogenase as a demonstration of enhanced sensitivity in covalent regulation
- 1 September 1983
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 305 (5932), 286-290
- https://doi.org/10.1038/305286a0
Abstract
The sensitivity to regulation of proteins undergoing covalent modification can be greatly increased when the substrates saturate the converter enzymes. This phenomenon, termed zero-order ultrasensitivity, occurs in the reversible phosphorylation of [Escherichia coli] isocitrate dehydrogenase. The possibility that this enhanced sensitivity is a common feature of covalent regulatory systems is discussed.This publication has 21 references indexed in Scilit:
- Insulin Receptor: Evidence That It Is a Protein KinaseScience, 1983
- Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free systemNature, 1982
- Amplification and Adaptation in Regulatory and Sensory SystemsScience, 1982
- An amplified sensitivity arising from covalent modification in biological systems.Proceedings of the National Academy of Sciences, 1981
- Interconvertible Enzyme Cascades in Cellular RegulationAnnual Review of Biochemistry, 1980
- Phosphorylation-Dephosphorylation of EnzymesAnnual Review of Biochemistry, 1979
- Evidence that the transforming gene of avian sarcoma virus encodes a protein kinase associated with a phosphoproteinCell, 1978
- Protein kinase activity associated with the avian sarcoma virus src gene product.Proceedings of the National Academy of Sciences, 1978
- Reversible Inactivation of the Isocitrate Dehydrogenase of Escherichia coli ML308 during Growth on AcetateJournal of General Microbiology, 1975
- Synthesis of C4-dicarboxylic acids from acetate by a “glyoxylate bypass” of the tricarboxylic acid cycleBiochimica et Biophysica Acta, 1957