Analysis of the Kinetics of the Enzyme-Catalysed Hydrolysis of an Ester

Multiple Choice

Analysis of the kinetics of the enzyme-catalysed hydrolysis of an ester by -chymotrypsin show that for an initial enzyme concentration of 4.5  10^-9 mol dm^-3, the maximum rate was 5.9  10^-13 mol dm^-3 s^-1 and the Michaelis constant was 5.6  10^-7 dm³ mol^-1. Calculate the efficiency of the enzyme.

A) 230 dm³ mol^-1 s^-1
B) 4.27  10^-3 dm³ mol^-1 s^-1
C) 1.36  10¹⁰ dm³ mol^-1 s^-1
D) 7.63  10³ dm³ mol^-1 s^-1