期刊
FEBS LETTERS
卷 587, 期 17, 页码 2778-2784出版社
WILEY
DOI: 10.1016/j.febslet.2013.07.031
关键词
Michaelis-Menten equation; Allosteric enzyme; Cooperativity; Oscillation; Systems biology
资金
- Fonds de la Recherche Scientifique Medicale (F.R.S.M., Belgium) [3.4607.99]
Oscillations occur in a number of enzymatic systems as a result of feedback regulation. How Michaelis-Menten kinetics influences oscillatory behavior in enzyme systems is investigated in models for oscillations in the activity of phosphofructokinase (PFK) in glycolysis and of cyclin-dependent kinases in the cell cycle. The model for the PFK reaction is based on a product-activated allosteric enzyme reaction coupled to enzymatic degradation of the reaction product. The Michaelian nature of the product decay term markedly influences the period, amplitude and waveform of the oscillations. Likewise, a model for oscillations of Cdc2 kinase in embryonic cell cycles based on Michaelis-Menten phosphorylation-dephosphorylation kinetics shows that the occurrence and amplitude of the oscillations strongly depend on the ultrasensitivity of the enzymatic cascade that controls the activity of the cyclin-dependent kinase. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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