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. 1969 Apr;62(4):1121–1128. doi: 10.1073/pnas.62.4.1121

NEGATIVE COOPERATIVITY IN REGULATORY ENZYMES*

Alexander Levitzki 1,†, D E Koshland Jr 1
PMCID: PMC223623  PMID: 5256410

Abstract

Negative cooperativity has been observed in CTP synthetase, an allosteric enzyme which contains a regulatory site. Thus, the same enzyme exhibits negative cooperativity for GTP (an effector) and glutamine (a substrate) and positive cooperativity for ATP and UTP (both substrates). In the process of the delineation of these phenomena, diagnostic procedures for negative cooperativity were developed. Application of these procedures to other enzymes indicates that negative cooperativity is a characteristic of many of them. These findings add strong support for the sequential model of subunit interactions which postulates that ligand-induced conformational changes are responsible for regulatory and cooperative phenomena in enzymes.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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