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 (Km, kcat) 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 Km app, kcat app, and [E]0 with monochlorodimedone as substrate, were obtained by using the linearization plot and the Vmax 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 Km value.
Toti P., Petri A., Pelaia V., Osman A.M., Paolini M., Bauer C. (2005). A linearization method for low catalytic activity enzyme kinetic analysis. BIOPHYSICAL CHEMISTRY, 114, 245-251.
A linearization method for low catalytic activity enzyme kinetic analysis.
PAOLINI, MORENO;
2005
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 (Km, kcat) 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 Km app, kcat app, and [E]0 with monochlorodimedone as substrate, were obtained by using the linearization plot and the Vmax 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 Km value.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
