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A linearization method for low catalytic activity enzyme kinetic analysis.

Paolo Toti·Antonella Petri·Valerio Pelaia·Ahmed M Osman·Moreno Paolini·Carlo Bauer
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Abstract

A kinetic analysis was made and a linear plot based on the general rate equation derived by Laidler [Can. J. Chem. 33, 1614-1624] is proposed. This linearization method allows determining the kinetic parameters (K(m), k(cat)) and [E](0) for enzymes with low catalytic activity. The method was applied to chloroperoxidase from Caldariomyces fumago [EC 1.11.1.10], whose kinetic parameters K(m)(app), k(cat)(app), and [E](0) with monochlorodimedone as substrate, were obtained by using the linearization plot and the V(max) value (calculated by Eadie-Hofstee plot). This plot could also be useful to the study of abenzyme kinetics provided the concentration of the latter is either higher or equal than K(m) value.

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CatalysisChloride PeroxidaseFungiKineticsLinear ModelsJournal Article

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Paolo Toti, Antonella Petri, Valerio Pelaia, Ahmed M Osman, Moreno Paolini, Carlo Bauer. 2005-01-05. A linearization method for low catalytic activity enzyme kinetic analysis.. https://doi.org/10.1016/j.bpc.2004.12.043

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