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Yeast glycolytic oscillations that are not controlled by a single oscillophore: A new definition of oscillophore strength

dc.contributor.authorReijenga K.A.
dc.contributor.authorVan Megen Y.M.G.A.
dc.contributor.authorKooi B.W.
dc.contributor.authorBakker B.M.
dc.contributor.authorSnoep J.L.
dc.contributor.authorVan Verseveld H.W.
dc.contributor.authorWesterhoff H.V.
dc.date.accessioned2011-05-15T15:59:50Z
dc.date.available2011-05-15T15:59:50Z
dc.date.issued2005
dc.identifier.citationJournal of Theoretical Biology
dc.identifier.citation232
dc.identifier.citation3
dc.identifier.issn225193
dc.identifier.other10.1016/j.jtbi.2004.08.019
dc.identifier.urihttp://hdl.handle.net/10019.1/11389
dc.description.abstractBiochemical oscillations, such as glycolytic oscillations, are often believed to be caused by a single so-called 'oscillophore'. The main characteristics of yeast glycolytic oscillations, such as frequency and amplitude, are however controlled by several enzymes. In this paper, we develop a method to quantify to which extent any enzyme determines the occurrence of oscillations. Principles extrapolated from metabolic control analysis are applied to calculate the control exerted by individual enzymes on the real and imaginary parts of the eigenvalues of the Jacobian matrix. We propose that the control exerted by an enzyme on the real part of the smallest eigenvalue, in terms of absolute value, quantifies to which extent that enzyme contributes to the emergence of instability. Likewise the control exerted by an enzyme on the imaginary part of complex eigenvalues may serve to quantify the extent to which that enzyme contributes to the tendency of the system to oscillate. The method was applied both to a core model and to a realistic model of yeast glycolytic oscillations. Both the control over stability and the control over oscillatory tendency were distributed among several enzymes, of which glucose transport, pyruvate decarboxylase and ATP utilization were the most important. The distributions of control were different for stability and oscillatory tendency, showing that control of instability does not imply control of oscillatory tendency nor vice versa. The control coefficients summed up to 1, suggesting the existence of a new summation theorem. These results constitute proof that glycolytic oscillations in yeast are not caused by a single oscillophore and provide a new, subtle, definition for the oscillophore strength of an enzyme. © 2004 Elsevier Ltd. All rights reserved.
dc.subjectadenosine triphosphate
dc.subjectenzyme activity
dc.subjectyeast
dc.subjectarticle
dc.subjectcontrolled study
dc.subjectcorrelation coefficient
dc.subjectenzyme activity
dc.subjectenzyme stability
dc.subjectfrequency analysis
dc.subjectfungal genetics
dc.subjectfungal metabolism
dc.subjectglycolysis
dc.subjectmathematical computing
dc.subjectmolecular biology
dc.subjectnonhuman
dc.subjectoscillation
dc.subjectpriority journal
dc.subjectprotein synthesis
dc.subjecttechnique
dc.subjectBiological Clocks
dc.subjectGlycolysis
dc.subjectModels, Biological
dc.subjectPhosphofructokinases
dc.subjectYeasts
dc.titleYeast glycolytic oscillations that are not controlled by a single oscillophore: A new definition of oscillophore strength
dc.typeArticle
dc.description.versionArticle


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