Negative cooperativity in regulatory enzymes.

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.

authors

Levitzki A,Koshland DE Jr

doi

10.1073/pnas.62.4.1121

subject

Has Abstract

pub_date

1969-04-01 00:00:00

pages

1121-8

issue

4

eissn

0027-8424

issn

1091-6490

journal_volume

62

pub_type

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