Determine the values of KM and Vmax for the

decarboxylation of a beta-keto acid given the

following data:
Substrate concentration Velocity
(moles L-1) (mM min-1)
2.500 0.588
1.000 0.500
0.714 0.417
0.526 0.370
0.250 0.256
The hydrolysis of a phenylalanine-containing
peptide is catalyzed by alpha-chymotrypsin
with the following results. Calculate Km and
Vmax for the reaction.
Peptide concentration Velocity
(M) (M min-1)
2.5 x 10-4 2.2 x 10-6
5.0 x 10-4 3.8 x 10-6
10.0 x 10-4 5.9 x 10-6
15.0 x 10-4 7.1 x 10-6
 Draw the Lineweaver-Burk Plots for the behavior of an enzyme
for which the following experimental data are available :

[S] v, No inhibitor v, with Inhibitor

(mm) (nmol min-1) (nmol min-1)
3.0 4.58 3.66
5.0 6.40 5.12
7.0 7.72 6.18
9.0 8.72 6.98
11.0 9.50 7.60

What are the Km and Vmax values for the inhibited and
uninhibited reactions? What type of inhibition is it?
For the following aspartase reaction, in the
presence of the inhibitor hydroxymethyl-
aspartate, determine Km and whether the
inhibition is competitive or non-competitive.
[S] v, no inhibitor v, with inhibitor
M arbitrary units arbitrary units
1 x 10-4 0.026 0.010
5 x 10-4 0.092 0.040
1.5 x 10-3 0.136 0.086
2.5 x 10-3 0.150 0.120
5 x 10-3 0.165 0.142