Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1988637 | Journal of Biochemical and Biophysical Methods | 2006 | 10 Pages |
Abstract
Isothermal titration calorimetry (ITC) has been applied to the determination of the activity of d-hydantoinase (EC 3.5.2.2) with several substrates by monitoring the heat released during the reaction. The method is based on the proportionality between the reaction rate and the thermal power (heat/time) generated. Microcalorimetric assays carried out at different temperatures provided the dependence of the catalytic rate constant on temperature. We show that ITC assay is a nondestructive method that allows the determination of the catalytic rate constant (kcat), Michaelis constant (KM), activation energy and activation Gibbs energy, enthalpy and entropy of this reaction.
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Authors
Montserrat Andújar-Sánchez, Francisco Javier Las Heras-Vázquez, Josefa María Clemente-Jiménez, Sergio Martínez-Rodríguez, Ana Camara-Artigas, Felipe Rodríguez-Vico, Vicente Jara-Pérez,