Oscillations in coupled enzymic reactions at high concentration of enzyme
Ryde-Pettersson, Ulf LU
(1992)
In BBA - Protein Structure and Molecular Enzymology
1119(2).
p.118-122
- Abstract
The transient-state kinetic consequences of the coupling of a single-enzyme reaction to other metabolic reactions have been examined in generalized terms. Analytical data are presented which specify under what conditions such coupling may lead to an oscillatory transient rate behaviour of a reaction system involving an enzyme operating by a Michaelian mechanism. The results indicate that the presence of enzyme in concentrations comparable to those of substrate and product may represent a hitherto unforeseen possible source of weakly damped, or even sustained, oscillations in metabolic networks. This observation has some important implications with regard to the occurrence of oscillations in biochemical reaction systems and to... (More)
The transient-state kinetic consequences of the coupling of a single-enzyme reaction to other metabolic reactions have been examined in generalized terms. Analytical data are presented which specify under what conditions such coupling may lead to an oscillatory transient rate behaviour of a reaction system involving an enzyme operating by a Michaelian mechanism. The results indicate that the presence of enzyme in concentrations comparable to those of substrate and product may represent a hitherto unforeseen possible source of weakly damped, or even sustained, oscillations in metabolic networks. This observation has some important implications with regard to the occurrence of oscillations in biochemical reaction systems and to transient-state kinetic modelling of metabolic systems.
(Less)
- author
- Ryde-Pettersson, Ulf
LU
- organization
- publishing date
- 1992-02-26
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- End-product inhibition, High enzyme concentration, Metabolic oscillation, Ribulose 1,5-bisphosphate carboxylase, Steady-state approximation
- in
- BBA - Protein Structure and Molecular Enzymology
- volume
- 1119
- issue
- 2
- pages
- 5 pages
- publisher
- Elsevier
- external identifiers
-
- pmid:1540642
- scopus:0026529511
- ISSN
- 0167-4838
- DOI
- 10.1016/0167-4838(92)90380-V
- language
- English
- LU publication?
- yes
- id
- 98ac949e-b4da-4481-a3ec-045a27221487
- date added to LUP
- 2017-02-04 11:16:57
- date last changed
- 2024-01-13 12:57:58
@article{98ac949e-b4da-4481-a3ec-045a27221487,
abstract = {{<p>The transient-state kinetic consequences of the coupling of a single-enzyme reaction to other metabolic reactions have been examined in generalized terms. Analytical data are presented which specify under what conditions such coupling may lead to an oscillatory transient rate behaviour of a reaction system involving an enzyme operating by a Michaelian mechanism. The results indicate that the presence of enzyme in concentrations comparable to those of substrate and product may represent a hitherto unforeseen possible source of weakly damped, or even sustained, oscillations in metabolic networks. This observation has some important implications with regard to the occurrence of oscillations in biochemical reaction systems and to transient-state kinetic modelling of metabolic systems.</p>}},
author = {{Ryde-Pettersson, Ulf}},
issn = {{0167-4838}},
keywords = {{End-product inhibition; High enzyme concentration; Metabolic oscillation; Ribulose 1,5-bisphosphate carboxylase; Steady-state approximation}},
language = {{eng}},
month = {{02}},
number = {{2}},
pages = {{118--122}},
publisher = {{Elsevier}},
series = {{BBA - Protein Structure and Molecular Enzymology}},
title = {{Oscillations in coupled enzymic reactions at high concentration of enzyme}},
url = {{http://dx.doi.org/10.1016/0167-4838(92)90380-V}},
doi = {{10.1016/0167-4838(92)90380-V}},
volume = {{1119}},
year = {{1992}},
}