The substrate of this enzyme is rich in positive charged chemical groups. On the surface of this protein there are two hydrophilic clusters and a solvent (water) -exposed hydrophobic pocket. One of the hydrophilic clusters is rich in negatively charged amino acids; the other one is rich in positively charged amino acids. Identify the active site of this enzyme by introducing mutations that affect the catalytic activity would you mutate a. Any of the surface hydrophilic clusters b. The surface hydrophilic cluster riches in positively charged amino acids c. The surface hydrophilic cluster riches in negatively charged amino acids d. The surface hydrophobic pocket