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Evolution of Enzyme Regulator Sites: Evidence for Partial Gene Duplication from Amino-acid Sequence of Bovine Glutamate Dehydrogenase

Nature volume 241, pages 118–120 (1973)Cite this article

Abstract

MODULATION of the biological activity of proteins by metabolite levels is a widespread and well-documented phenomenon. As Monod, Wyman and Changeux1 pointed out, most regulatory protein molecules are composed of several subunits. The regulation of some oligomeric proteins, notably haemoglobin2, involves interaction of similar sites on separate similar subunits. In other cases such as that of aspartate transcarbamylase3 there are separate catalytic and regulatory subunits. Some proteins, however, possess within individual subunits both active sites and regulatory sites capable of mediating homotropic and/or heterotropic interaction.

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  1. Department of Biochemistry, University of Sheffield, S10 2TN

    P. C. ENGEL

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  1. P. C. ENGEL
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ENGEL, P. Evolution of Enzyme Regulator Sites: Evidence for Partial Gene Duplication from Amino-acid Sequence of Bovine Glutamate Dehydrogenase. Nature 241, 118–120 (1973). https://doi.org/10.1038/241118a0

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