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 metalloprotease.

Chemistry
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Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
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Chapter1: Chemical Foundations
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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 metalloprotease.
Metalloproteases
B:
H
R₁
HN
R₂
Zn
2+
Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the
structures, click More followed by Reset Drawing.
Transcribed Image Text: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 metalloprotease. Metalloproteases B: H R₁ HN R₂ Zn 2+ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing.
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