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A steady state mathematical model for stepwise “slow-binding” reversible enzyme inhibition
- Source :
-
Analytical Biochemistry . Sep2008, Vol. 380 Issue 1, p5-12. 8p. - Publication Year :
- 2008
-
Abstract
- Abstract: The standard mathematical model for stepwise “slow-binding” enzyme inhibition assumes that the initial enzyme–inhibitor complex is always at equilibrium with the free component species and . This assumption implies that the dissociation rate constant is infinitely higher than the isomerization rate constant for . This paper presents a more general mathematical treatment, under the steady state approximation rather than the usual rapid-equilibrium approximation, whereby the two rate constants for the disappearance of are allowed to be comparable in magnitude. Experimentally relevant illustrative examples include discrimination between a single-step and a two-step mechanism for slow-binding inhibition kinetics. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 00032697
- Volume :
- 380
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Analytical Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 33139267
- Full Text :
- https://doi.org/10.1016/j.ab.2007.11.027