Intrasteric regulation of protein kinases and phosphatases

Biochim Biophys Acta. 1991 Aug 13;1094(1):67-76. doi: 10.1016/0167-4889(91)90027-u.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites*
  • Molecular Sequence Data
  • Phosphoric Monoester Hydrolases / chemistry
  • Phosphoric Monoester Hydrolases / metabolism*
  • Protein Kinases / chemistry
  • Protein Kinases / metabolism*
  • Substrate Specificity


  • Protein Kinases
  • Phosphoric Monoester Hydrolases