The kinetics of asymmetric reduction of acetyltrimethylsilane and its carbon analogue catatlyzed by horse liver alcohol dehydrogenase were explored. It has been found that the relation between substrate concentration and initial reaction rate was in accordance with the Michaelis-Menten equation when enzyme concentration was below 150 mg/L and the K_m, v_max and E_a of HLADH-catalyzed asymmetric reduction of acetyltrimethylsilane were 2.67 mmol/L, 0.118 mmol/(L·min·mg) and 37 kJ/mol respectively, while the corresponding parameters for its carbon analogue were 3.56 mmol/L, 0.084 mmol/(L·min·mg) and 61 kJ/mol.