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PMID: 14685773 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Quasi-steady state assumptions for non-isolated enzyme-catalysed reactions.

Journal of mathematical biology ·Vol. 48 ·No. 1 ·2004-01-00 ·Pages 82-104

Stoleriu I, Davidson FA, Liu JL

Abstract

The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme-catalysed biochemical reactions is studied. Almost all previous work has concentrated on isolated reactions, i.e. those without input or other environmental influences. In this paper, we investigate the effects of substrate input on this formulation, in particular, on the nature and validity of the quasi-steady state assumptions.

MeSH Terms
Algorithms Catalysis Data Interpretation, Statistical Enzymes/chemistry Kinetics Models, Chemical Substrate Specificity
Chemicals
Enzymes
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Stoleriu I
Department of Mathematics, University of Dundee, Dundee, DD1 4HN, Scotland, UK.
Davidson F A
Liu J L
References (6)
6 references, click to expand
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  3. On the validity of the steady state assumption of enzyme kinetics.
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  4. Enzyme kinetics at high enzyme concentration.
    Bull Math Biol. 2000 May;62(3):483-99 PMID: 10812718
  5. Extending the quasi-steady state approximation by changing variables.
    Bull Math Biol. 1996 Jan;58(1):43-63 PMID: 8819753
  6. Mathematical modelling of dynamics and control in metabolic networks. I. On Michaelis-Menten kinetics.
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Article Info
Journal
Journal of mathematical biology
Abbr.
J Math Biol
ISSN
0303-6812
Published
2004-01-00
Epub
2003-00-20
Pages
82-104
Language
English
Region
Germany
NLM ID
7502105
Subset
IM
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