glyceraldehyde phosphate dehydrogenase [TDH3]
glyceraldehyde phosphate dehydrogenase [TDH2]
glyceraldehyde phosphate dehydrogenase [TDH1]
reversible michaelis-menten: ordered bi-bi
reversible michaelis-menten: two substrates, two products, three inhibitors, non-competitive inhibition
reversible michaelis-menten: one substrate, one product
irreversible michaelis-menten: one substrate, no product
Smallbone2013 - Glycolysis in S.cerevisiae - Iteration 12
Smallbone2013 - Glycolysis in S.cerevisiae - Iteration 12 This model is described in the article: A model of yeast glycolysis based on a consistent kinetic characterization of all its enzymes Kieran Smallbone, Hanan L. Messiha, Kathleen M. Carroll, Catherine L. Winder, Naglis Malys, Warwick B. Dunn, Ettore Murabito, Neil Swainston, Joseph O. Dada, Farid Khan, Pınar Pir, Evangelos Simeonidis, Irena Spasić, Jill Wishart, Dieter Weichart, Neil W. Hayes, Daniel Jameson, David S. Broomhead, Stephen G. Oliver, Simon J. Gaskell, John E.G. McCarthy, Norman W. Paton, Hans V. Westerhoff, Douglas B. Kell, Pedro Mendes FEBS Letters (in press) Abstract: We present an experimental and computational pipeline for the generation of kinetic models of metabolism, and demonstrate its application to glycolysis in Saccharomyces cerevisiae. Starting from an approximate mathematical model, we employ a “cycle of knowledge” strategy, identifying the steps with most control over flux. Kinetic parameters of the individual isoenzymes within these steps are measured experimentally under a standardised set of conditions. Experimental strategies are applied to establish a set of in vivo concentrations for isoenzymes and metabolites. The data are integrated into a mathematical model that is used to predict a new set of metabolite concentrations and reevaluate the control properties of the system. This bottom-up modelling study reveals that control over the metabolic network most directly involved in yeast glycolysis is more widely distributed than previously thought. This model is hosted on BioModels Database and identified by: MODEL1303260012 . To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models . To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.
reversible michaelis-menten: two noncompeting couples
facilitated diffusion: symmetrical carrier
reversible michaelis-menten: ordered uni-bi
irreversible michaelis-menten: two substrates, no products