The individual steps in the Michaelis-Menten enzyme mechanism involve all of the following EXCEPT:
a. The rateconstant k-2 can be ignored since no P is present to convert backto S, when the initial velocity (Vo) is measured
b. k1 is the rateconstant for formation of the ES complex from E and S
c. The step in themechanism involving k2 is much faster than the step involving k1 /k -1
d. k2 is the rateconstant for the catalytic step in which S is converted to P in theactive site of the enzyme
e. k -1 is therate constant for dissociation of S from the ES complex