Kinetic analysis of protein modification reactions at equilibrium.
A kinetic analysis is presented of reactions of protein modification, and/or of modification-induced enzyme inactivation, which can formally be described by a single exponential function, or by a summation of two exponential functions, of reaction time plus a constant term. The reaction schemes compatible with the kinetic formalism of these cases are given, and a simple kinetic criterion is described whereby the identification of one of these cases, strong negative protein modification co-operativity, may be carried out. The treatment outlined in this paper is applied to a case from the literature, the inactivation of glyceraldehyde-3-phosphate dehydrogenase by butane-2,3-dione [Asriyants, Benkevich & Nagradova (1983) Biokhimiya (Engl. Transl.) 48, 164-171].
Rakitzis
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Department of Biological Chemistry, University of Athens Medical School, Greece.
D000818:Animals; D004852:Epoxy Compounds; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D066298:In Vitro Techniques; D007700:Kinetics; D011506:Proteins; D011817:Rabbits; D051381:Rats; D013816:Thermodynamics
D004852:Epoxy Compounds; D011506:Proteins; C007366:diepoxybutane; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases