Resumen

ARANDA, J. S.  y  SALGADO, E.. Enzymatic catalysis modelling with allosteric enzymes. Rev. Mex. Ing. Quím [online]. 2008, vol.7, n.1, pp.21-27. ISSN 1665-2738.

Allosteric enzymes control reaction rates in biochemical reactions. The catalytic activity of allosteric enzymes depends on the concentration of a certain regulating compound. A simgoidal saturation curve is a characteristic of the enzymes that exert allosteric control of reaction rates. These enzymes are rather large enzymatic complexes usually composed of at least one catalytic subunit and a regulatory fraction, and the complex catalytic activity is given by the cooperative interactions between those enzymatic subunits. Realistic simulation of biocatalytic allosteric phenomena requires an appropiate modelling of the enzyme kinetic behavior. Modelling enzymes with cooperative kinetics can be achieved by defining interacting agents. Agent-based modelling allows an accurate representation of sigmoidal saturation curves, without the kinetic parameters that are needed in other kinetic models. Experimental data from Escherichia coli aspartate transcarbamylase are compared to theoretical results from different models for allosteric systems. Results from agent-based modelling show a good agreement with experimental saturation curves.

Palabras llave : enzymatic reactions; allosteric enzymes; enzyme kinetics; agent-based modelling.

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