REAGENT-INDUCED CHANGES IN THE STRUCTURE AND CATALYTIC ACTIVITY OF GLUTAMIC DEHYDROGENASE

Abstract
Glutamic dehydrogenase has been presented as a model where control of an enzyme function is related to control of its structure. Glutamic dehydrogenase is responsive to a number of small regulator molecules which bind in a highly specific manner and induce conformational changes in the enzyme molecule. Regulation of the enzyme structure is, in several instances, a multivalent process and requires the simultaneous binding of more than one regulator molecule. Conformational changes on disaggregation of the enzyme induced by various regulator reagents as well as dilution have been shown to correlate with stimulation of alanine dehydrogenase activity of the crystalline enzyme, confirming the conclusion that such changes in the molecule are important variables in determining enzymic activity.

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