Encyclopedia of Computational Neuroscience

Living Edition
| Editors: Dieter Jaeger, Ranu Jung

Modeling of Enzyme Kinetics

  • Kim T. Blackwell
Living reference work entry
DOI: https://doi.org/10.1007/978-1-4614-7320-6_187-1


Mathematical formulation of the rates of chemical reactions that are catalyzed by enzymes, which are molecules that are regenerated as part of the chemical reaction.

Detailed Description

Models of reaction–diffusion systems consist of bimolecular reactions, enzyme reactions, and diffusion. An enzyme is a molecule that facilitates a reaction or transformation of a substrate molecule into a different molecule(s), known as the product. For example, ATP can be transformed into cAMP + PPi spontaneously at an extremely low rate; adenylyl cyclase is an enzyme that greatly facilitates the transformation. The theory behind enzyme reactions is that a large energy barrier prevents a reaction from occurring spontaneously, and the enzyme lowers the energy barrier.

Enzyme reactions are modeled as a series of elementary reactions. First, the enzyme ( E) and substrate ( S) bind to each other to form the enzyme-substrate complex ( ES). Second, the substrate is transformed into the products....


Enzyme Reaction Adenylyl Cyclase Bimolecular Reaction Inositol Triphosphate Uncompetitive Inhibition 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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  1. Brown SA, Morgan F, Watras J, Loew LM (2008) Analysis of phosphatidylinositol-4,5-bisphosphate signaling in cerebellar Purkinje spines. Biophys J 95(4):1795–1812PubMedCrossRefPubMedCentralGoogle Scholar
  2. Chen WW, Niepel M, Sorger PK (2010) Classic and contemporary approaches to modeling biochemical reactions. Genes Dev 24(17):1861–1875PubMedCrossRefPubMedCentralGoogle Scholar
  3. Ciliberto A, Capuani F, Tyson JJ (2007) Modeling networks of coupled enzymatic reactions using the total quasi-steady state approximation. PLoS Comput Biol 3(3):e45PubMedCrossRefPubMedCentralGoogle Scholar
  4. Dessauer CW, Gilman AG (1997) The catalytic mechanism of mammalian adenylyl cyclase. Equilibrium binding and kinetic analysis of P-site inhibition. J Biol Chem 272(44):27787–27795PubMedCrossRefGoogle Scholar
  5. Macnamara S, Bersani AM, Burrage K, Sidje RB (2008) Stochastic chemical kinetics and the total quasi-steady-state assumption: application to the stochastic simulation algorithm and chemical master equation. J Chem Phys 129(9):095105PubMedCrossRefGoogle Scholar
  6. Stenesh J (1992) Core topics in biochemistry. Cogno Press, KalamazooGoogle Scholar
  7. Tzafriri AR, Edelman ER (2005) On the validity of the quasi-steady state approximation of bimolecular reactions in solution. J Theor Biol 233(3):343–350PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  1. 1.Molecular Neuroscience Department, Krasnow Institute for Advanced StudyGeorge Mason UniversityFairfaxUSA