Difference between revisions of "DXR"
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== Modelling DXR == | == Modelling DXR == | ||
− | DXR is modelled reversible with the Michaelis-Menten rate law using Hanekom's generic random order bi-bi equation <ref name="Hanekom2016"> [http://scholar.sun.ac.za/ Hanekom, A. J. 2006.] "Generic kinetic equations for modelling multisubstrate reactions in computational systems biology", MSc Thesis submitted at the University of Stellenbosch</ref>. There are a total of five kinetic parameters (2 forward Kms, 2 reverse Kms and 1 Kcat), and one thermodynamic parameter (Equilibrium constant , Keq). | + | DXR is modelled reversible with the Michaelis-Menten rate law using Hanekom's generic random order bi-bi equation <ref name="Hanekom2016"> [http://scholar.sun.ac.za/ Hanekom, A. J. 2006.] "Generic kinetic equations for modelling multisubstrate reactions in computational systems biology", MSc Thesis submitted at the University of Stellenbosch</ref> <ref name="Sauro"> Sauro, H.M. "Enzyme kinetics for systems biology"</ref>. There are a total of five kinetic parameters (2 forward Kms, 2 reverse Kms and 1 Kcat), and one thermodynamic parameter (Equilibrium constant , Keq). |
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Revision as of 16:24, 23 March 2017
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DXR reaction
The 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR, EC 1.1.1.267) is the second step in the MEP pathway that catalyses the production of 2-C-methyl-D-erythritol 4-phosphate (MEP) from 1-deoxy-D-xylulose 5-phosphate (DXP).
Modelling DXR
DXR is modelled reversible with the Michaelis-Menten rate law using Hanekom's generic random order bi-bi equation [1] [2]. There are a total of five kinetic parameters (2 forward Kms, 2 reverse Kms and 1 Kcat), and one thermodynamic parameter (Equilibrium constant , Keq).
References
- ↑ Hanekom, A. J. 2006. "Generic kinetic equations for modelling multisubstrate reactions in computational systems biology", MSc Thesis submitted at the University of Stellenbosch
- ↑ Sauro, H.M. "Enzyme kinetics for systems biology"