The kinetic effect of the inactivation of the enzyme--substrate complex in an enzymatic reaction with slow-binding inhibition

DOI10.1016/J.AMC.2005.01.042zbMATH Open1080.92032OpenAlexW1967775989MaRDI QIDQ814739FDOQ814739

Authors: C. Garrido-del Solo, J. M. Yago, M. Garcia-Moreno, Bent H. Havsteen, Francisco Garcia-Cánovas, R. Varon 

Publication date: 7 February 2006

Published in: Applied Mathematics and Computation (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1016/j.amc.2005.01.042

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zbMATH Keywords

Enzyme inhibitionEnzyme reactionsInactivationRapid equilibriumSlow-binding inhibition

Mathematics Subject Classification ID

Dynamical systems in biology (37N25) Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45)

Cites Work

• Klassische Runge-Kutta-Formeln vierter und niedrigerer Ordnung mit Schrittweiten-Kontrolle und ihre Anwendung auf Wärmeleitungsprobleme

Cited In (4)

• Kinetic behaviour of proenzymes activation in the presence of different inhibitors for both activating and activated enzymes
• The ``memory effect in a chain of biochemical reactions with a positive feedback is enhanced by substrate saturation described by Michaelis-Menten kinetics
• Equilibrium competition binding assay: inhibition mechanism from a single dose response
• Kinetic study of an enzyme-catalysed reaction in the presence of novel irreversible-type inhibitors that react with the product of enzymatic catalysis

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