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Biochemistry Module
Enzyme kinetics inhibitors Worksheet
1. From this graph determine the KM and Vmax?
2. How would the rate of product formation change if:
? the substrate concentration were doubled?
? the enzyme concentration were doubled?
3. What is the value of the Michaelis-Menten equation ,when the substrate concentration, [S],
equals the Km (i.e., the Michaelis constant)?
A) v0 = Vmax / 2
B) v0= Vmax/ [S]2
C) v0 = Vmax* [S]
D) v0 = Vmax * Km
4. For a Michaelis-Menten enzyme, the Y-axis intercept on a double-reciprocal plot equals:
A) 1/Km
B) Km
C) -1/Km
D) -Km
E) V max
F) 1/Vmax
5. Using the provided graph, If Vmax = 3 mM/s for a Michaelis-Menten enzyme, what is the
velocity (in mM/s) when [S] = Km = 10mM?
6. The flowchart provided shows the action of the enzyme
phosphofructokinase (PFK) in the production of ATP through the reactions
involved in respiration.
ATP can bind to an allosteric site on PFK to reduce the enzymeàactivity. What is
this process an example of?
?
A Anabolic inhibition
?
B Catabolic inhibition
?
C Positive feedback
?
D Competitive inhibition
?
E End product inhibition
7. Which of the following diagrams shows the action of a noncompetitive inhibitor for this enzyme?
8. The diagram shows
an enzyme-catalyzed
reaction that is taking
place in the presence of
an inhibitor.
The rate of reaction has
slowed. How could the
rate of reaction be increased?
?
A By adding more inhibitors
?
B By decreasing the temperature
?
C By adding more substrates
?
D By adding a different inhibitor
9. Another effective treatment for methanol poisoning is fomepizole, a
competitive inhibitor of the alcohol dehydrogenase enzyme. Illustrate the effect
of fomepizole on the conversion of methanol to formaldehyde (methanol
poisoning) by drawing the comparative M-M curve and LB plot below (i.e. draw
the methanol curves when fomepizole is added to the assay).
Questions 10,11

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