Concept explainers
(a)
Interpretation:
The mechanism for peptide bond cleavage by a cysteine protease should be completed.
Concept introduction:
In peptide bond hydrolysis, the strategy of the protease is to generate a nucleophile that attacks the peptide carbonyl group. In cysteine protease, a cysteine residue is activated by a histidine residue and this activated cysteine act as the nucleophile that attacks the peptide bond.
(b)
Interpretation:
The mechanism for peptide bond cleavage by an aspartyl protease should be completed.
Concept introduction:
In aspartyl protease active site there are two aspartic residues which allow a water molecule to attack the peptide bond. One aspartic acid residue activates the water molecule, polarizes the peptide carbonyl group so that it is susceptible to attack.
(c)
Interpretation:
The mechanism for peptide bond cleavage by metalloproteases should be completed.
Concept introduction:
The active site of the metalloprotease is composed of a bound metal ion. This metal ion activates a water molecule in order to perform a nucleophilic attack on peptide carbonyl carbon.
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