The activation of chymotrypsinogen, a zymogen, requires the cleavage of a bond between arg-15 and ile-16, and the subsequent attraction of ile-16 and asp-194. complete parts (a) and (b). complete the reaction for the proteolytic cleavage of arg‑15 and ile‑16 at ph 7.6. specify the enzyme that catalyzes the reaction and modify the given structure to form the products. the dipeptide arginine isoleucine is treated with water and an enzyme to form the products. the dipeptide backabone consists of r bonded to n h bonded to the alpha carbon of arg bonded to a carbonyl bonded to n h bonded to the alpha carbon of isoleucine bonded to a carbonyl bonded to r 1. the side chain of arginine is c h 2 c h 2 c h 2 n h c n h 2. the last c is also double bonded to n h 2 plus. the side chain of isoleucine is c h bonded to methyl and ethyl.