Literature DB >> 1530568

An easy method for deriving steady-state rate equations.

S G Waley1.   

Abstract

The scope and limitations of a simple and satisfactory method of deducing steady-state rate equations is described. This method (called the Flux Method) consists in writing down the flux in successive steps of the reaction, and calculating the relative concentration of enzyme forms and thence the turnover time. Kinetic mechanisms for linear and branched pathways are used as examples of this method.

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Year:  1992        PMID： 1530568      PMCID： PMC1132905          DOI： 10.1042/bj2860357

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  4 in total

1.  Partition analysis and the concept of net rate constants as tools in enzyme kinetics.

Authors:  W W Cleland
Journal:  Biochemistry       Date:  1975-07-15       Impact factor: 3.162

2.  A COMPARISON OF ESTIMATES OF MICHAELIS-MENTEN KINETIC CONSTANTS FROM VARIOUS LINEAR TRANSFORMATIONS.

Authors:  J E DOWD; D S RIGGS
Journal:  J Biol Chem       Date:  1965-02       Impact factor: 5.157

3.  Accumulation of acyl-enzyme in DD-peptidase-catalysed reactions with analogues of peptide substrates.

Authors:  M Jamin; M Adam; C Damblon; L Christiaens; J M Frère
Journal:  Biochem J       Date:  1991-12-01       Impact factor: 3.857

4.  Evolutionary optimization of the catalytic effectiveness of an enzyme.

Authors:  J J Burbaum; R T Raines; W J Albery; J R Knowles
Journal:  Biochemistry       Date:  1989-11-28       Impact factor: 3.162
  4 in total
  1 in total

1.  The role of high-dimensional diffusive search, stabilization, and frustration in protein folding.

Authors:  Supreecha Rimratchada; Tom C B McLeish; Sheena E Radford; Emanuele Paci
Journal:  Biophys J       Date:  2014-04-15       Impact factor: 4.033
  1 in total

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