Question

Studies conducted with a lysozyme mutant that contains an Asp -> Asn change at position 52 and a Glu -> Gln change at position 35 exhibited almost a complete loss in enzymatic activity. What is the most likely explanation for the decrease in enzyme activity in the mutant?

A) increased affinity for substrate
B) absence of negative charges in the active site
C) change in the active-site scaffold
D) larger amino acids in the active site decreases the affinity for substrate

Answer 1

The most likely explanation for the decrease in enzymatic activity in the lysozyme mutant is a C) change in the active-site scaffold. Hence, C) is correct.

Step-by-step explanation:

The most likely explanation for the decrease in enzymatic activity in the lysozyme mutant with the Asp -> Asn change at position 52 and the Glu -> Gln change at position 35 is a change in the active-site scaffold. The active site of an enzyme is the specific region where the substrate binds and the catalytic reaction occurs.

The amino acid residues in the active site play a crucial role in catalysis, and any changes in these residues can disrupt the proper folding and conformation of the active site, leading to a loss in enzymatic activity.