Applying structural transition theory to describe enzyme kinetics in heterogeneous systems

DOI10.1007/S10910-014-0325-1MaRDI QIDQ460904zbMATHOpenAlexFDO

Authors Marília L. C. Silva, Ivo H. P. Andrade, Giovani B. M. Carvalho, Jose Ailton Conceicao Bispo, Carlos Francisco Sampaio Bonafe

Publication date 9 October 2014

Published in Journal of Mathematical Chemistry (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1007/s10910-014-0325-1

zbMATH Keywords

Michaelis-Menten kineticsenzyme kineticsHMM and MWC modelstwo-state model

Mathematics Subject Classification ID

Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45)

Recommendations

• Enzyme kinetics of multiple alternative substrates
• Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond
• Extending the kinetic solution of the classic Michaelis--Menten model of enzyme action
• Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation
• Quasi-steady state assumptions for non-isolated enzyme-catalysed reactions

Cites work

• Asymptotic expansions in enzyme reactions with high enzyme concentrations
• Enzyme kinetics at high enzyme concentration
• Extending the kinetic solution of the classic Michaelis--Menten model of enzyme action
• Michaelis-Menten kinetics at high enzyme concentrations
• Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation

Cited in

(9)

• scientific article; zbMATH DE number 4053412 (Why is no real title available?)
• On the relationship between the Hill coefficients for steady-state and transient kinetic data: a criterion for concerted transitions in allosteric proteins
• Multifractality in intracellular enzymatic reactions
• Two new regulatory properties arising from the transient phase kinetics of monocyclic enzyme cascades
• A study of the temperature dependence of bienzyme systems and enzymatic chains
• Programming substrate-independent kinetic barriers with thermodynamic binding networks
• New features of the steady-state rate related with the initial concentration of substrate in the diphenolase and monophenolase activities of tyrosinase
• A further step in the kinetic characterisation of the tyrosinase enzymatic system
• Docking and Molecular Dynamics Simulation of Complexes of High and Low Reactive Substrates with Peroxidases

This page was built for publication: Applying structural transition theory to describe enzyme kinetics in heterogeneous systems

Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q460904)