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PMID: 1653024 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Intrasteric regulation of protein kinases and phosphatases.

Biochimica et biophysica acta ·Vol. 1094 ·No. 1 ·1991-08-13 ·Pages 67-76

Kemp BE, Pearson RB

Abstract

Protein kinases and protein phosphatases are the pre-eminent regulators of cellular processes. Many of these enzymes are present in latent forms that are activated by various modulators. The inhibited form is maintained by autoinhibitory domains either within these proteins or in some instances by separate inhibitory subunits. A number of these autoinhibitory structures have been identified because of structural similarity to their enzyme's substrate. These findings indicate that the enzyme's active site may recognize either substrates or pseudosubstrate autoinhibitory structures that turn them off. Because this form of regulation is directed at the active site it is termed intrasteric control.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Molecular Sequence Data Phosphoric Monoester Hydrolases/chemistry,metabolism Protein Kinases/chemistry,metabolism Substrate Specificity
Chemicals
Protein Kinases Phosphoric Monoester Hydrolases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kemp B E
St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Pearson R B
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1991-08-13
Pages
67-76
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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