In an enzyme's active site, a catalytic histidine residue abstracts a proton from the hydroxyl group of a catalytic serine residue. The catalytic serine then performs a nucleophilic attack on the carbonyl carbon of a peptide bond (on the substrate). The final products of this reaction are a cleaved substrate at the peptide bond, with a new amino group and carboxyl group, and regenerated catalytic residues. In this reaction, the serine residue is displaying what?   A. Proximity and Orientation B. Covalent catalysis C. Metal ion catalysis D .A and B E. B and C F. None stated here

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