A new serine protease was discovered that preferentially cleaves a peptide bond

Question

A new serine protease was discovered that preferentially cleaves a peptide bond adjoining a negatively charged side chain.  Which of the following is true?                       

                            a.              It likely reacts much faster than chymotrypsin                             b.              The specificity pocket is likely lined with amino acids such as Arg and Lys                             c.              The specificity pocket would mimic that of trypsin                             d.              It likely reacts much slower than chymotrypsin                             e.              The specificity pocket would mimic that of chymotrypsin

Explanation / Answer

reason = chymotrypsin's specificity pocket: is lined with small hydrophobic side chains, leaving considerable room in the nonpolar pocket

b. The specificity pocket is likely lined with amino acids such as Arg and Lys

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