Mechanisms of the Aspartoacylase Catalytic Activity Regulation According to the Computer Modeling Results

Abstract

The results of molecular modeling allow us to associate the catalytic activity of aspartoacylase towards the hydrolysis of N-acetylaspartate with the dynamic properties of a dimeric molecule of the enzyme. The availability of the enzyme’s active site for the substrate is controlled by the conformational dynamics of the peptide loops that form a gate to the transport channel in one of the monomers. It is shown that this model explains the results of the experimental studies according to which the point mutation K213E does not affect the catalytic function of the enzyme.