Literature DB >> 3230366

Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios.

C L Frenzen1, P K Maini.   

Abstract

We extend the validity of the quasi-steady state assumption for a model double intermediate enzyme-substrate reaction to include the case where the ratio of initial enzyme to substrate concentration is not necessarily small. Simple analytical solutions are obtained when the reaction rates and the initial substrate concentration satisfy a certain condition. These analytical solutions compare favourably with numerical solutions of the full system of differential equations describing the reaction. Experimental methods are suggested which might permit the application of the quasi-steady state assumption to reactions where it may not have been obviously applicable before.

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Year:  1988        PMID: 3230366     DOI: 10.1007/bf00276148

Source DB:  PubMed          Journal:  J Math Biol        ISSN: 0303-6812            Impact factor:   2.259


  4 in total

1.  Minimization of intermediate concentrations as a suggested optimality principle for biochemical networks. II. Time hierarchy, enzymatic rate laws, and erythrocyte metabolism.

Authors:  S Schuster; R Schuster; R Heinrich
Journal:  J Math Biol       Date:  1991       Impact factor: 2.259

2.  On the validity of the steady state assumption of enzyme kinetics.

Authors:  L A Segel
Journal:  Bull Math Biol       Date:  1988       Impact factor: 1.758

3.  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

4.  Exploiting Bioprocessing Fluctuations to Elicit the Mechanistics of De Novo Lipogenesis in Yarrowia lipolytica.

Authors:  Andreas E Vasdekis; Andrew M Silverman; Gregory Stephanopoulos
Journal:  PLoS One       Date:  2017-01-04       Impact factor: 3.240

  4 in total

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