Abstract: In this study，the chiral selectivity of arginase was investigated by means of molecular dynamics and molecular docking. According to comparing the L-type arginine–arginaseⅠcomplex and D-type arginine–arginaseⅠcomplex, it was observed that L-type arginine–arginase complex had higher stability. From the results of the molecular dynamics trajectories of two complexes, it was shown that the L-type Arginine–Arginase complex had a RMSD curve with less shock and higher energy level than the D-type Arginine–arginase complex. Above all, the conclusion was drawn that the chiral selectivity of Arginine in the catalytic reaction was thoroughly depended on the structure of the enzyme active domain.

Key words: molecular dynamics, molecule docking, chiral, arginase