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

DOI10.1016/J.AMC.2005.01.042MaRDI QIDQ814739zbMATHOpenAlexFDO

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

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)

Recommendations

• Kinetic behaviour of proenzymes activation in the presence of different inhibitors for both activating and activated enzymes
• Kinetic study of an enzyme-catalysed reaction in the presence of novel irreversible-type inhibitors that react with the product of enzymatic catalysis
• VALIDITY OF THE QUASI STEADY STATE ASSUMPTION FOR ENZYME-CATALYSED REACTIONS WITH COMPETITIVE INHIBITION AND SUBSTRATE INPUT
• Solution of the Haldane equation for substrate inhibition enzyme kinetics using the decomposition method
• Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond
• Enzyme kinetics: a critique of the quasi-steady-state approximation
• Quasi-steady state kinetics of simple sequential multienzyme reactions with single substrates
• Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios
• scientific article; zbMATH DE number 7410335
• Kinetics of a general model for enzyme activation through a limited proteolysis

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

This page was built for publication: The kinetic effect of the inactivation of the enzyme--substrate complex in an enzymatic reaction with slow-binding inhibition

Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q814739)