Final answer:
If the catalytic triad aspartate in the active site of trypsin is mutated to asparagine, the activity of trypsin would decrease significantly.c. Decrease significantly
Step-by-step explanation:
The catalytic triad in the active site of trypsin consists of three amino acids: histidine, serine, and aspartate. These three amino acids work together to form the active site and catalyze the enzymatic reaction. Aspartate plays a crucial role in the catalytic mechanism by stabilizing the catalytic intermediate. If the catalytic triad aspartate is mutated to asparagine, it would affect the activity of trypsin.
Asparagine is a nonpolar, hydrophobic amino acid that lacks the negatively charged carboxyl group present in aspartate. This change in the amino acid residue could disrupt the hydrogen bonding interactions and electrostatic interactions essential for catalytic activity. As a result, the activity of trypsin would decrease significantly.
Therefore, if the catalytic triad aspartate is mutated to asparagine, the activity of trypsin would decrease significantly.