Final answer:
A mutation from Glycine to Threonine in Chymotrypsin affects the enzyme's substrate affinity and catalytic efficiency, altering parameters like KM and kcat/KM.
Step-by-step explanation:
The mutation of Glycine 216 to Threonine on Chymotrypsin most likely has a significant impact on the enzyme's functionality. The amino acid change can alter the enzyme's active site and thus its affinity for substrates and its catalytic efficiency. KM (Michaelis constant) is a measure of the enzyme's substrate affinity: the lower the KM, the higher the affinity. kcat (turnover number) is the number of substrate molecules an enzyme can convert into product per unit time when the enzyme is saturated with substrate. The question refers to how these parameters might change for chymotrypsin, a protease enzyme, when glycine is replaced by threonine due to a mutation.
According to the provided information, mutation of Glycine 216 to Threonine on Chymotrypsin will most likely decrease the kcat/Km for Chymotrypsin and increase the KM for N-Acetyltyrosine ethyl ester. Therefore, the correct answer is option c) Decrease the kcat/Km; N-Acetylglycine ethyl ester.