Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a Cysteine protease. H Cysteine proteases N R₂ HN R₁

Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a Cysteine protease. H Cysteine proteases N R₂ HN R₁

Chemistry & Chemical Reactivity

10th Edition

ISBN:9781337399074

Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Chapter14: Chemical Kinetics: The Rates Of Chemical Reactions

Section14.7: Reaction Mechanisms

Problem 1.1ACP

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The following data were recorded from an experiment to measure the activity of a peptidase enzyme. A number of solutions of different concentrations of a dipeptide were prepared then the same small amount of the enzyme was added to each of them. The rate of cleavage of the peptide bond was measured and the initial rate of the reaction was recorded Peptide conc (mmol L-¹) 0.334 0.450 0.667 1.00 1.33 1.67 Initial rate 0.152 0.201 0.269 0.417 0.505 0.667 (mmol L¹ s¹) For the peptidase enzyme find the maximum velocity and the Michaelis constant.
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As you increase the temperature of an enzyme-catalyzedreaction, the rate of the reaction initially increases. It thenreaches a maximum rate and finally dramatically declines.Keeping in mind that enzymes are proteins, how do youexplain these changes in reaction rate?