Literature DB >> 16850351

The total quasi-steady-state approximation for fully competitive enzyme reactions.

Morten Gram Pedersena1, Alberto M Bersani, Enrico Bersani.   

Abstract

The validity of the Michaelis-Menten-Briggs-Haldane approximation for single enzyme reactions has recently been improved by the formalism of the total quasi-steady-state approximation. This approach is here extended to fully competitive systems, and a criterion for its validity is provided. We show that it extends the Michaelis-Menten-Briggs-Haldane approximation for such systems for a wide range of parameters very convincingly, and investigate special cases. It is demonstrated that our method is at least roughly valid in the case of identical affinities. The results presented should be useful for numerical simulations of many in vivo reactions.

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Year:  2006        PMID: 16850351     DOI: 10.1007/s11538-006-9136-2

Source DB:  PubMed          Journal:  Bull Math Biol        ISSN: 0092-8240            Impact factor:   1.758


  7 in total

1.  Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity.

Authors:  Morten Gram Pedersen; Alberto Maria Bersani
Journal:  J Math Biol       Date:  2009-03-31       Impact factor: 2.259

2.  Enhanced identification and exploitation of time scales for model reduction in stochastic chemical kinetics.

Authors:  Carlos A Gómez-Uribe; George C Verghese; Abraham R Tzafriri
Journal:  J Chem Phys       Date:  2008-12-28       Impact factor: 3.488

3.  Michaelis-Menten speeds up tau-leaping under a wide range of conditions.

Authors:  Sheng Wu; Jin Fu; Yang Cao; Linda Petzold
Journal:  J Chem Phys       Date:  2011-04-07       Impact factor: 3.488

4.  Adaptive deployment of model reductions for tau-leaping simulation.

Authors:  Sheng Wu; Jin Fu; Linda R Petzold
Journal:  J Chem Phys       Date:  2015-05-28       Impact factor: 3.488

5.  Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics.

Authors:  Justin Eilertsen; Wylie Stroberg; Santiago Schnell
Journal:  J Theor Biol       Date:  2019-01-05       Impact factor: 2.691

6.  The quasi-steady-state approximations revisited: Timescales, small parameters, singularities, and normal forms in enzyme kinetics.

Authors:  Justin Eilertsen; Santiago Schnell
Journal:  Math Biosci       Date:  2020-03-14       Impact factor: 2.144

7.  Modeling networks of coupled enzymatic reactions using the total quasi-steady state approximation.

Authors:  Andrea Ciliberto; Fabrizio Capuani; John J Tyson
Journal:  PLoS Comput Biol       Date:  2007-03-16       Impact factor: 4.475

  7 in total

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