PMID: 8947485Nov 15, 1996Paper

Kinetics of inactivation of bovine pancreatic ribonuclease A by bromopyruvic acid

The Biochemical Journal
M H WangK Y Zhao

Abstract

The kinetic theory of substrate reaction during the modification of enzyme activity [Duggleby (1986) J. Theor. Biol. 123, 67-80; Wang and Tsou (1990) J. Theor. Biol. 142, 531-549] has been applied to a study of the inactivation kinetics of ribonuclease A by bromopyruvic acid. The results show that irreversible inhibition belongs to a non-competitive complexing type inhibition. On the basis of the kinetic equation of substrate reaction in the presence of the inhibitor, all microscopic kinetic constants for the free enzyme, the enzyme-substrate complex and the enzyme-product complex have been determined. The non-competitive inhibition type indicates that neither the substrate nor the product affects the binding of bromopyruvic acid to the enzyme and that the ionization state of His-119 may be the same in both the enzyme-substrate and the enzyme-product complexes.

Citations

Jun 18, 2017·Organic & Biomolecular Chemistry·John T M DiMaioBradley L Nilsson
Aug 9, 2003·The Journal of Biological Chemistry·Hao Wu, Zhi-Xin Wang
Nov 20, 2019·Chembiochem : a European Journal of Chemical Biology·Nesrin Vurgun, Mark Nitz

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