Literature DB >> 2039478

How to draw kinetic barrier diagrams for enzyme-catalysed reactions.

J Südi1.   

Abstract

A modified way to construct kinetic barrier diagrams is presented. Although the diagram superficially resembles a free-energy profile, it is independent of any conception derived from transition-state theory. Some simple calculations referring to the lactate dehydrogenase turnover reaction at equilibrium demonstrate self-consistency of the diagram and its direct relevance to the results of numerical simulations of the detailed course of enzyme-catalysed reactions.

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Year:  1991        PMID: 2039478      PMCID: PMC1151175          DOI: 10.1042/bj2760265

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


  5 in total

1.  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

2.  Rate of isotope exchange in enzyme-catalyzed reactions.

Authors:  G Yagil; H D Hoberman
Journal:  Biochemistry       Date:  1969-01       Impact factor: 3.162

3.  Mathematical treatment of enzyme-catalyzed isotope-exchange reactions.

Authors:  J Flossdorf; M R Kula
Journal:  Eur J Biochem       Date:  1972-10

4.  The lactate dehydrogenase--reduced nicotinamide--adenine dinucleotide--pyruvate complex. Kinetics of pyruvate binding and quenching of coeznyme fluorescence.

Authors:  J Südi
Journal:  Biochem J       Date:  1974-04       Impact factor: 3.857

5.  Macroscopic rate constants involved in the formation and interconversion of the two central enzyme--substrate complexes of the lactate dehydrogenase turnover.

Authors:  J Südi
Journal:  Biochem J       Date:  1974-04       Impact factor: 3.857

  5 in total
  2 in total

1.  Kinetic barriers under steady-state conditions.

Authors:  J Südi
Journal:  Biochem J       Date:  1992-05-15       Impact factor: 3.857

2.  Control analysis applied to single enzymes: can an isolated enzyme have a unique rate-limiting step?

Authors:  G C Brown; C E Cooper
Journal:  Biochem J       Date:  1993-08-15       Impact factor: 3.857

  2 in total

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