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Compare and contrast serine proteases and aspartic proteases. Not all answers will be used: Serine protease Both Aspartic protease catalylic triad of serine. histidine. and aspartic acid (WO asparlic acids in aclive site tetrahedral intermediate covalent intermediale direct nucleophilic attack by water Answer Bank trigonal planar intermediate four aspartic acids in active site direct electrophilic attack by water catalytic triad of serine, leucine, and valine
Compare and contrast serine proteases and aspartic proteases. Not all answers will be used: Serine protease Both Aspartic protease catalylic triad of serine. histidine. and aspartic acid (WO asparlic acids in aclive site tetrahedral intermediate covalent intermediale direct nucleophilic attack by water Answer Bank trigonal planar intermediate four aspartic acids in active site direct electrophilic attack by water catalytic triad of serine, leucine, and valine
Serine proteases and aspartic proteases are two types ofproteolytic enzymesthat cleave peptide bonds in proteins, but they differ in their mechanism of action and the residues involved in catalysis.Serine proteasesuse a catalytic triad of serine, histidine, and aspartic acid to cleave the peptide bond. The serine residue acts as a nucleophile and attacks the carbonyl carbon of the peptide bond, forming a covalent intermediate. The histidine residue stabilizes the negative charge of the intermediate, while the aspartic acid residue stabilizes the positive charge of the leaving amino group. A water molecule then attacks the intermediate, cleaving the peptide bond.Aspartic proteases, on the other hand, use four aspartic acid residues in the active site to stabilize the tetrahedral intermediate and facilitate the cleavage of the peptide bond. The carbonyl oxygen of the peptide bond coordinates with two of the aspartic acid residues, while the nitrogen of the peptide bond coordinates with the other two aspartic acid residues. This creates a trigonal planar intermediate that is susceptible to direct electrophilic attack by water.In summary, serine proteases and aspartic proteases use different residues and mechanisms of action to catalyze the cleavage of peptide bonds. Serine proteases use a catalytic triad of serine, histidine, and aspartic acid, while aspartic proteases use fouraspartic acid residues.To learn more aboutProteolytic enzymesbrainly.com/question/30336809#SPJ4...