Exercises-on-enzymes.ppt

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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] (mm) 3.0 5.0 7.0 9.0 11.0

v, No inhibitor (nmol min-1) 4.58 6.40 7.72 8.72 9.50

v, with Inhibitor (nmol min-1) 3.66 5.12 6.18 6.98 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 hydroxymethylaspartate, 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

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