Reference no: EM132439761

Problem: Steady state kinetic parameters for the cleavage of different polypeptide-like substrates by a serine protease are shown in the table below. Each substrate contains a single cleavable peptide bond with different amino acid residues present in the Rn-1 position. The concentration of enzyme is identical in all reactions. Residue in Rn-1 position KM (µM) kcat/KM (s-1 µM-1) 

Arginine 2.0 50 

Valine 10.0 10 

Aspartic Acid 100.0 1 

Which statement provides the BEST explanation for these observations? 

A. The enzyme has the highest affinity for the aspartic acid-containing substrate.

B. The catalytic efficiency is highest for the aspartic acid-containing substrate.

C. The rate of the k2 step for the arginine-containing substrate is significantly greater than for the valine-containing substrate.

D. 50% of Vmax for the valine-containing substrate was reached at a lower substrate concentration than for the arginine-containing substrate.

E. At a substrate concentration of 2 µM, the arginine-containing substrate will produce a higher concentration of ES complex than the other two substrates.