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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
chemistry
Kinetic and thermodynamic aspects of enzyme control and regulation
Journal of Physical Chemistry B, Volume 114, No. 49, Year 2010
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Description
This paper develops concepts for assessing and quantifying the regulation of the rate of an enzyme-catalyzed reaction. We show how generic reversible rate equations can be recast in two ways, one making the distance from equilibrium explicit, thereby allowing the distinction between kinetic and thermodynamic control of reaction rate, as well as near-equilibrium and far-from-equilibrium reactions. Recasting in the second form separates mass action from rate capacity and quantifies the degree to which intrinsic mass action contributes to reaction rate and how regulation of an enzyme-catalyzed reaction either enhances or counteracts this massaction behavior. The contribution of enzyme binding to regulation is analyzed in detail for a number of enzyme-kinetic rate laws, including cooperative reactions. © 2010 American Chemical Society.
Authors & Co-Authors
Rohwer, Johann M.
South Africa, Stellenbosch
Triple-j Group for Molecular Cell Physiology
Hofmeyr, J. H.S.
South Africa, Stellenbosch
Triple-j Group for Molecular Cell Physiology
South Africa, Stellenbosch
Stellenbosch University
Statistics
Citations: 32
Authors: 2
Affiliations: 2
Identifiers
Doi:
10.1021/jp108412s
ISSN:
15206106
e-ISSN:
15205207