Question

How much activity (in terms of relative k_cat values) does the version of subtilisin with all three residues in the catalyic triad mutated have compared to uncatalyzed reaction? Propose an explanation.

Answer 1

The bacterial Serine subtilisin show that when all three residues of the catalytic triad are mutated, the catalytic rate of enzyme is 3000 times the uncatalysed reaction rate

i.e.., K_cat/K_uncat = 3000

Substilisin belongs to subtilases, a group of serine proteases. Subtilinsin is an extracellular alkaline serine protease, it catalyses the hydrolysis of proteins and peptide amides.

The activity of the version of subtilisin with all three residues in the catalytic triad mutated have compared to uncatalyzed reaction is 3000.