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Enzyme Activity: Allosteric Regulation

  1. Thomas Traut

Published Online: 28 SEP 2007

DOI: 10.1002/9780470015902.a0000865.pub2



How to Cite

Traut, T. 2007. Enzyme Activity: Allosteric Regulation. eLS. .

Author Information

  1. University of North Carolina School of Medicine, Chapel Hill, North Carolina, USA

Publication History

  1. Published Online: 28 SEP 2007

This is not the most recent version of the article. View current version (15 MAY 2014)


Cells can respond to changes in their environment by altering the flow through particular metabolic pathways. Such a change in any metabolic step is due to certain key enzymes that have the ability to alter their rate of activity. Such enzymes are defined as allosteric. The extent to which these enzymes adopt either the active conformation or the inactive conformation depends on their response to appropriate positive or negative signals. An easily measured feature of allosteric enzymes is the cooperativity that they show in a kinetic experiment.


  • allosteric;
  • conformation;
  • enzyme;
  • negative cooperativity;
  • positive cooperativity;
  • regulation