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cooperativity

Interaction between the substrate binding sites of an allosteric enzyme. Binding of a substrate molecule to one binding site changes the affinity of the binding sites on the other subunits (cf. allosteric enzymes) to the substrate by induction of a conformation change at the other binding sites. Cooperative enzymes typically display a sigmoid (S-shaped) plot of the reaction rate against substrate concentration.
Source:
PAC, 1992, 64, 143 (Glossary for chemists of terms used in biotechnology (IUPAC Recommendations 1992)) on page 151
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IUPAC. Compendium of Chemical Terminology, 2nd ed. (the "Gold Book"). Compiled by A. D. McNaught and A. Wilkinson. Blackwell Scientific Publications, Oxford (1997). XML on-line corrected version: http://goldbook.iupac.org (2006-) created by M. Nic, J. Jirat, B. Kosata; updates compiled by A. Jenkins. ISBN 0-9678550-9-8. doi:10.1351/goldbook.
Last update: 2014-02-24; version: 2.3.3.
DOI of this term: doi:10.1351/goldbook.C01325.
Original PDF version: http://www.iupac.org/goldbook/C01325.pdf. The PDF version is out of date and is provided for reference purposes only. For some entries, the PDF version may be unavailable.
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