Tutorial: Enzyme Kinetics

1. Why is the rate of an enzyme-catalyzed reaction proportional to the amount of E.S

complex?

2. During an experiment, students at first Year College of Medicine discovered a new enzyme
called COM-20. The enzyme had a Vmax of 150 micromoles (mM) product formed per minute
by a milligram of enzyme. The KM for the major substrate of the enzyme is 1.5 mM.
a) What is the initial reaction rate (vo) when the [S] is 0.5 mM?
b) What is the initial reaction rate (vo) when the [S] is 3.0 mM?
c) What is the initial reaction rate (vo) when the [S] is 15.0 mM?

3. Pharmaceutical sciences students showed at in a particular enzyme-catalyzed reaction was

Vmax = 0.2 mol/sec and Km = 5 mM. Assume the enzyme shows standard Michaelis-Menten
kinetics. What is the rate of the reaction when [S] = 10 mM?

4. A medical analyst working on enzymes found that an enzyme she hydrolyzed had a
substrate concentration of 0.03 mmol/L, the initial velocity was 1.5x10-3 mmol/L.min-1 and
the maximum velocity was 4.5x10-3 mmol/L.min-1 . Calculate the km value.

5. Foundation students were experimenting on kinetics of an enzyme in the presence and

absence of an inhibitor. The following data were obtained for an enzyme in the absence of
an inhibitor and in the presence of an inhibitor.
[S] V(set 1) V(set 2)
(mM) (µmol/sec) (µmol/sec)
1 8.6 24
2 16 40
4 28 58
10 42 70

On the same graph, draw Lineweaver-Burke plot of the reaction kinetics, labeling the axes
and giving values for the two points where each line crosses the axes. Calculate the Km and
Vmax.