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PMID: 6312317 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Phosphorylation of isocitrate dehydrogenase as a demonstration of enhanced sensitivity in covalent regulation.

Nature ·Vol. 305 ·No. 5932 ·1983-00-00 ·Pages 286-90

LaPorte DC, Koshland DE

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, has been found to occur in the reversible phosphorylation of isocitrate dehydrogenase. The possibility that this enhanced sensitivity is a common feature of covalent regulatory systems is discussed.

MeSH Terms
Allosteric Regulation Enzyme Activation Isocitrate Dehydrogenase/metabolism Kinetics Phosphoprotein Phosphatases/metabolism Phosphoproteins/metabolism Phosphorylation Protein Kinases/metabolism
Chemicals
Phosphoproteins Isocitrate Dehydrogenase Protein Kinases Phosphoprotein Phosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
LaPorte D C
Koshland D E
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1983-00-00
Pages
286-90
Language
English
Region
England
NLM ID
0410462
Subset
IM
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