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A New Approach for Determination of the Selectively Favoured Kinetic Design of Enzyme Reactions

Pettersson, Gösta LU (1996) In Journal of Theoretical Biology 183(2). p.179-183
Abstract
A new criterion is applied for characterization of the kinetic design of enzymes that should be favoured by a selective pressure in the direction of increased metabolic reaction flux. According to this criterion, the selectively favoured state of a metabolic sequence of enzyme reactions conforming to Michaelis-Menten kinetics is identical with the uniform one which is known to optimize reaction flux for a given average magnitude of enzyme concentrations and of true and apparent first-order rate constants in the reaction system. It is argued that presently observed values of on-velocity constants for metabolite binding to enzymes are unlikely to represent the upper limit for a diffusion-controlled association process and are more likely to... (More)
A new criterion is applied for characterization of the kinetic design of enzymes that should be favoured by a selective pressure in the direction of increased metabolic reaction flux. According to this criterion, the selectively favoured state of a metabolic sequence of enzyme reactions conforming to Michaelis-Menten kinetics is identical with the uniform one which is known to optimize reaction flux for a given average magnitude of enzyme concentrations and of true and apparent first-order rate constants in the reaction system. It is argued that presently observed values of on-velocity constants for metabolite binding to enzymes are unlikely to represent the upper limit for a diffusion-controlled association process and are more likely to represent those corresponding to the selectively favoured kinetic design at the present stage of the evolutionary development of enzyme function. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Theoretical Biology
volume
183
issue
2
pages
179 - 183
publisher
Academic Press
external identifiers
  • scopus:0030597334
ISSN
1095-8541
DOI
10.1006/jtbi.1996.0211
language
English
LU publication?
yes
id
46db12e4-ebe3-4bd9-ade0-594400d2ec67 (old id 126329)
date added to LUP
2007-07-06 14:07:22
date last changed
2017-01-01 06:43:05
@article{46db12e4-ebe3-4bd9-ade0-594400d2ec67,
  abstract     = {A new criterion is applied for characterization of the kinetic design of enzymes that should be favoured by a selective pressure in the direction of increased metabolic reaction flux. According to this criterion, the selectively favoured state of a metabolic sequence of enzyme reactions conforming to Michaelis-Menten kinetics is identical with the uniform one which is known to optimize reaction flux for a given average magnitude of enzyme concentrations and of true and apparent first-order rate constants in the reaction system. It is argued that presently observed values of on-velocity constants for metabolite binding to enzymes are unlikely to represent the upper limit for a diffusion-controlled association process and are more likely to represent those corresponding to the selectively favoured kinetic design at the present stage of the evolutionary development of enzyme function.},
  author       = {Pettersson, Gösta},
  issn         = {1095-8541},
  language     = {eng},
  number       = {2},
  pages        = {179--183},
  publisher    = {Academic Press},
  series       = {Journal of Theoretical Biology},
  title        = {A New Approach for Determination of the Selectively Favoured Kinetic Design of Enzyme Reactions},
  url          = {http://dx.doi.org/10.1006/jtbi.1996.0211},
  volume       = {183},
  year         = {1996},
}