Inhibitory effect of different product analogues on b-alanine synthase: A thermodynamic and fluorescence analysis
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Andújar Sánchez, Montserrat![University of Almería authority University of Almería authority](/themes/Mirage2/images/autoridades/autoridad.png)
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Date
2009Abstract
The enzyme N-carbamoyl-b-alanine amidohydrolase catalyse the hydrolysis of N-carbamoyl-b-alanine or N-carbamoyl-b-aminoisobutyric acid to b-alanine or 3-aminoisobutyric acid, under the release of carbondioxide and ammonia. This work studies the inhibition of N-carbamoyl-b-alanine amidohydrolase from Agrobacterium tumefaciens C58 (Atbcar) by different carboxylic acid compounds that differ in number of carbons, and position and size of ramification, while the binding thermodynamics of the inhibitors
are studied by isothermal titration calorimetry (ITC) and fluorescence. From the binding constants and inhibition studies, we conclude that propionate is the most efficient inhibitor among those tested. Substitution of the linear alkyl acids in positions 2 and 3 resulted in a drastic decrease of the affinity. The thermodynamic parameters show that a conformational change is triggered upon ligand binding. Binding enthalpy DHb is negative in all cases for all ligands, and thus, Van der Waals i...
Palabra/s clave
Isothermal titration calorimetry
N-Carbamoyl-b-alanine amidohydrolase
b-Ureidopropionase
Fluorescence
Inhibition