TUTORIAL 4: ENZYMES

1.

How much faster is a reaction with the fastest enzyme than without a catalyst? A. B. C. D. About 100 times faster. About 1,000 times faster. About 10,000 times faster. About 1020 times faster.

2.

As catalysts, enzymes are A. B. C. D. significantly less effective than nonenzymatic catalysts slightly less effective than nonenzymatic catalysts significantly more effective than nonenzymatic catalysts slightly more effective than nonenzymatic catalysts

. .

3.

The rate of a reaction depends on A. B. C. D. the free energy change the activation energy the enthalpy change the entropy change

4.

What effect does a catalyst have on the G of a reaction? A catalyst lowers the G A catalyst raises the G A catalyst has no effect on the G It depend on the specific catalyst

A. B. C. D. 5.

Which of the following is true?

A. B. C. D.

The E-S complex often dissociates with no reaction taking place The E-S complex must form before a reaction can take place Once the E-S complex forms, it can go on to form product or dissociate to E+S All of the above

6. An aldolase enzyme, called fructose-bisphosphate aldolase, is an enzyme that cleaves the C-C bond in aldol (aldehyde alcohol). This enzyme is classified as A. B. C. D. Lyases hydrolases Ligases transferases

7.

Which of the following is TRUE about the graph?

A. B. C. D.

The type of inhibition is a competitive inhibitor. The inhibition is an irreversible inhibitor. Increasing the substrate concentration reverses the inhibition effect. The inhibitor decreases the maximum velocity of the enzyme.

8.

The kinetic data in the following table were obtained for the reaction of carbon dioxide and water to produce bicarbonate and hydrogen ion catalyzed by carbonic anhydrase: (Campbell no. 28) CO2 + H2O HCO3- + H+

From these data, determine KM and Vmax for the reaction. Plot an appropriate graph and show your calculation.

CO2 concentration (mmol/L) 1.25 2.5 5.0 20.0

1/Velocity (M-1 sec) 36 x 103 20 x 103 12 x 103 6 x 103

9. The hydrolysis of a phenylalanine-containing peptide is catalyzed by -chymotrypsin with following results. a) Calculate KM and Vmax for the reaction. : (Campbell no. 35) Peptide concentration (M) 2.5 x 10-4 5.0 x 10-4 10.0 x 10-4 15.0 x 10-4 1/Velocity (M/min) 2.2 x 10-6 5.8 x 10-6 5.9 x 10-6 7.1 x 10-6

b) Using your KM and Vmax values in (a), calculate the velocity of the reaction when the peptide concentration is 6.55 x 10-4. (Results varies depend on Km and Vmax values)

10. Draw Lineweaver-Burke plots fro teh behaviour of an enzyme for which the following experimental data are available. : (Campbell no. 55)

[S] (mM) 3 5 7 9 11

V, No Inhibitor (mmol/min) 4.58 6.40 7.72 8.72 9.50

V, Inhibitor Present (mmol/min) 3.66 5.12 6.18 6.98 7.60