Literature DB >> 8373361

Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.

C Garrido-del Solo1, F García-Cánovas, B H Havsteen, R Varón-Castellanos.   

Abstract

A kinetic analysis of the Michaelis-Menten mechanism is made for the cases in which the free enzyme, or the enzyme-substrate complex, or both, are unstable, either spontaneously or as a result of the addition of a reagent. The explicit time-course equations of all of the species involved has been derived under conditions of limiting enzyme concentration. The validity of these equations has been checked by using numerical simulations. An experimental design and a kinetic data analysis allowing the evaluation of the parameters and kinetic constants are recommended.

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Year:  1993        PMID： 8373361      PMCID： PMC1134476          DOI： 10.1042/bj2940459

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


  10 in total

1.  Analysis of residuals: criteria for determining goodness-of-fit.

Authors:  M Straume; M L Johnson
Journal:  Methods Enzymol       Date:  1992       Impact factor: 1.600

2.  Analysis of kinetic data for irreversible enzyme inhibition.

Authors:  P J Gray; R G Duggleby
Journal:  Biochem J       Date:  1989-01-15       Impact factor: 3.857

3.  Progress curves of reactions catalyzed by unstable enzymes. A theoretical approach.

Authors:  R G Duggleby
Journal:  J Theor Biol       Date:  1986-11-07       Impact factor: 2.691

4.  Transient-phase kinetics of enzyme inactivation induced by suicide substrates.

Authors:  J Tudela; F García Cánovas; R Varón; F García Carmona; J Gálvez; J A Lozano
Journal:  Biochim Biophys Acta       Date:  1987-04-30

Review 5.  Kinetics of substrate reaction during irreversible modification of enzyme activity.

Authors:  C L Tsou
Journal:  Adv Enzymol Relat Areas Mol Biol       Date:  1988

6.  Resistance to inactivation by EGTA of the enzyme-substrate and enzyme-phosphate complexes of alkaline phosphatase.

Authors:  S J Pike; R G Duggleby
Journal:  Biochem J       Date:  1987-06-15       Impact factor: 3.857

7.  Kinetics of suicide substrates. Practical procedures for determining parameters.

Authors:  S G Waley
Journal:  Biochem J       Date:  1985-05-01       Impact factor: 3.857

8.  An easy method for the determination of initial rates.

Authors:  S G Waley
Journal:  Biochem J       Date:  1981-03-01       Impact factor: 3.857

9.  Kinetics of suicide substrates.

Authors:  S G Waley
Journal:  Biochem J       Date:  1980-03-01       Impact factor: 3.857

10.  Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier.

Authors:  W X Tian; C L Tsou
Journal:  Biochemistry       Date:  1982-03-02       Impact factor: 3.162
  10 in total
  3 in total

1.  A novel approach to distinguish between enzyme mechanisms: quasi-steady-state kinetic analysis of the prostaglandin H synthase peroxidase reaction.

Authors:  Peter V Vrzheshch; Elena A Batanova; Alevtina T Mevkh; Sergei D Varfolomeev; Irina G Gazaryan; Roger N F Thorneley
Journal:  Biochem J       Date:  2003-06-15       Impact factor: 3.857

2.  Mechanism and kinetics of inducible nitric oxide synthase auto-S-nitrosation and inactivation.

Authors:  Brian C Smith; Nathaniel B Fernhoff; Michael A Marletta
Journal:  Biochemistry       Date:  2012-01-24       Impact factor: 3.162

3.  Kinetics of an enzyme reaction in which both the enzyme-substrate complex and the product are unstable or only the product is unstable.

Authors:  C Garrido-del Solo; F García-Cánovas; B H Havsteen; E Valero; R Varón
Journal:  Biochem J       Date:  1994-10-15       Impact factor: 3.857
  3 in total

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