A Quantum Chemical Study on The Catalytic Mechanism of Serine Proteases(Ⅰ) / 昆明医科大学学报

ABSTRACT

Using the semi-empirical MNDO/H method several systems simulating the reaction of tetrahetral intermediate formation in the active site of serine proteases have been studied. The role played by elements of the《catalytic triad》in increasing the reactivity of serine hydroxyl has been discussed.The formation of a strong hydrogen bond between His and Asp was shown to be important in lowering the activation energy in the reaction of Ser with substrate.The change in position of the proten located between Ser and His and between His and Asp was analysed.The influence of substrate distortion on the energy of intermediate formation has been considered.