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. 1993 Sep 1;294(Pt 2):459–464. doi: 10.1042/bj2940459

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

C Garrido-del Solo 1, F García-Cánovas 1, B H Havsteen 1, R Varón-Castellanos 1
PMCID: PMC1134476  PMID: 8373361

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Duggleby R. G. Progress curves of reactions catalyzed by unstable enzymes. A theoretical approach. J Theor Biol. 1986 Nov 7;123(1):67–80. doi: 10.1016/s0022-5193(86)80236-3. [DOI] [PubMed] [Google Scholar]
  2. Gray P. J., Duggleby R. G. Analysis of kinetic data for irreversible enzyme inhibition. Biochem J. 1989 Jan 15;257(2):419–424. doi: 10.1042/bj2570419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Pike S. J., Duggleby R. G. Resistance to inactivation by EGTA of the enzyme-substrate and enzyme-phosphate complexes of alkaline phosphatase. Biochem J. 1987 Jun 15;244(3):781–785. doi: 10.1042/bj2440781. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Straume M., Johnson M. L. Analysis of residuals: criteria for determining goodness-of-fit. Methods Enzymol. 1992;210:87–105. doi: 10.1016/0076-6879(92)10007-z. [DOI] [PubMed] [Google Scholar]
  5. Tian W. X., Tsou C. L. Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier. Biochemistry. 1982 Mar 2;21(5):1028–1032. doi: 10.1021/bi00534a031. [DOI] [PubMed] [Google Scholar]
  6. Tsou C. L. Kinetics of substrate reaction during irreversible modification of enzyme activity. Adv Enzymol Relat Areas Mol Biol. 1988;61:381–436. doi: 10.1002/9780470123072.ch7. [DOI] [PubMed] [Google Scholar]
  7. Tudela J., García Cánovas F., Varón R., García Carmona F., Gálvez J., Lozano J. A. Transient-phase kinetics of enzyme inactivation induced by suicide substrates. Biochim Biophys Acta. 1987 Apr 30;912(3):408–416. doi: 10.1016/0167-4838(87)90046-x. [DOI] [PubMed] [Google Scholar]
  8. Waley S. G. An easy method for the determination of initial rates. Biochem J. 1981 Mar 1;193(3):1009–1012. doi: 10.1042/bj1931009. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Waley S. G. Kinetics of suicide substrates. Practical procedures for determining parameters. Biochem J. 1985 May 1;227(3):843–849. doi: 10.1042/bj2270843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Waley S. G. Kinetics of suicide substrates. Biochem J. 1980 Mar 1;185(3):771–773. doi: 10.1042/bj1850771. [DOI] [PMC free article] [PubMed] [Google Scholar]

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