Literature DB >> 1008809

Simplifications of the derivations and forms of steady-state equations for non-equilibrium random substrate-modifier and allosteric enzyme mechanisms.

E P Whitehead.   

Abstract

The steady-state equations for "random" enzymic mechanisms (ones with alternative routes for substrate and enzyme to form enzyme-substrate complexes) are non-Michaelian and very complicated when a quasi-equilibrium approximation cannot be used. General methods for simplifying their forms and derivations are given and applied to several single-substrate mechanisms of general or topical interest. The special simplifications resulting from partial ordering of reaction mechanism, from gross inequalities of rate constants, and from special relationships between catalytic and dissociation rate constants, are considered with reference to allosteric mechanisms. Some equations mentioned, but not given here, and more detailed working out of some of those given, have been deposited as Supplementary Publication SUP 50069 (18 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms given in Biochem. J. (1976) 153, 5.

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Year:  1976        PMID: 1008809      PMCID: PMC1164140          DOI: 10.1042/bj1590449a

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


  13 in total

1.  The presence of protein bound intermediates in the biosynthesis of gramicidin S.

Authors:  T I. Jones; O Vaage; T L. Zimmer; L O. Frøholm; S G. Laland
Journal:  FEBS Lett       Date:  1968-10       Impact factor: 4.124

2.  TREATMENT OF ENZYME KINETIC DATA. I. THE EFFECT OF MODIFIERS ON THE KINETIC PARAMETERS OF SINGLE SUBSTRATE ENZYMERS.

Authors:  C FRIEDEN
Journal:  J Biol Chem       Date:  1964-10       Impact factor: 5.157

3.  ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

Authors:  J MONOD; J WYMAN; J P CHANGEUX
Journal:  J Mol Biol       Date:  1965-05       Impact factor: 5.469

4.  A Note on the Kinetics of Enzyme Action.

Authors:  G E Briggs; J B Haldane
Journal:  Biochem J       Date:  1925       Impact factor: 3.857

5.  Possible implications for allosteric models of hemoglobin of the laws of combination with carbon monoxide under photodissociating conditions.

Authors:  E Whitehead
Journal:  Biophys Chem       Date:  1974-12       Impact factor: 2.352

6.  Carbon monoxide binding by hemoglobin and myoglobin under photodissociating conditions.

Authors:  M Brunori; J Bonaventura; C Bonaventura; E Antonini; J Wyman
Journal:  Proc Natl Acad Sci U S A       Date:  1972-04       Impact factor: 11.205

7.  Interpretation of the binding of carbon monoxide to hemoglobin under photodissociating conditions.

Authors:  A Szabo; M Karplus
Journal:  Proc Natl Acad Sci U S A       Date:  1973-03       Impact factor: 11.205

8.  Subunit interactions in enzyme catalysis. Kinetic analysis of subunit interactions in the enzyme L-phenylalanine ammonia-lyase.

Authors:  J Nari; C Mouttet; F Fouchier; J Ricard
Journal:  Eur J Biochem       Date:  1974-02-01

9.  Subunit interactions in enzyme catalysis. Kinetic models for one-substrate polymeric enzymes.

Authors:  J Ricard; C Mouttet; J Nari
Journal:  Eur J Biochem       Date:  1974-02-01

10.  A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state.

Authors:  S Cha
Journal:  J Biol Chem       Date:  1968-02-25       Impact factor: 5.157

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  6 in total

1.  In defence of the general validity of the Cha method of deriving rate equations. The importance of explicit recognition of the thermodynamic box in enzyme kinetics.

Authors:  C M Topham; K Brocklehurst
Journal:  Biochem J       Date:  1992-02-15       Impact factor: 3.857

2.  A computer program for enzyme kinetics that combines model discrimination, parameter refinement and sequential experimental design.

Authors:  R Franco; M T Gavaldà; E I Canela
Journal:  Biochem J       Date:  1986-09-15       Impact factor: 3.857

3.  Patterns of apparent co-operativity in a simple random non-equilibrium enzyme--substrate--modifier mechanism. Comparison with equilibrium allosteric models.

Authors:  E P Whitehead; M R Egmond
Journal:  Biochem J       Date:  1979-02-01       Impact factor: 3.857

4.  Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine oxidase, chymotrypsin, fumarase, galactose dehydrogenase, beta-galactosidase, lactate dehydrogenase, peroxidase and xanthine oxidase.

Authors:  W G Bardsley; P Leff; J Kavanagh; R D Waight
Journal:  Biochem J       Date:  1980-06-01       Impact factor: 3.857

5.  On an alleged exception to generalized microscopic reversibility as a condition for reduction in degree of steady-state kinetic equations.

Authors:  E P Whithead
Journal:  Biochem J       Date:  1981-11-01       Impact factor: 3.857

6.  Generalized microscopic reversibility, kinetic co-operativity of enzymes and evolution.

Authors:  J Ricard
Journal:  Biochem J       Date:  1978-12-01       Impact factor: 3.857

  6 in total

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