Applying structural transition theory to describe enzyme kinetics in heterogeneous systems
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Publication:460904
DOI10.1007/S10910-014-0325-1zbMATH Open1296.92111OpenAlexW1969784536MaRDI QIDQ460904FDOQ460904
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
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Cites Work
- Michaelis-Menten kinetics at high enzyme concentrations
- Asymptotic expansions in enzyme reactions with high enzyme concentrations
- Extending the kinetic solution of the classic Michaelis--Menten model of enzyme action
- Enzyme kinetics at high enzyme concentration
- Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation
Cited In (8)
- Docking and Molecular Dynamics Simulation of Complexes of High and Low Reactive Substrates with Peroxidases
- Title not available (Why is that?)
- On the relationship between the Hill coefficients for steady-state and transient kinetic data: a criterion for concerted transitions in allosteric proteins
- A study of the temperature dependence of bienzyme systems and enzymatic chains
- A further step in the kinetic characterisation of the tyrosinase enzymatic system
- 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
- Two new regulatory properties arising from the transient phase kinetics of monocyclic enzyme cascades
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