A recent discovery has suggested that a gene mutation results in several amino acid substitutions within an active site. The following substitutions have been identified and are each expected to properly fold and form the active site: Normal protein amino acids Valine Leucine Valine Substitutions Lysine Arginine Arginine Deleted and replaced with a coenzyme capable of covalent binding Histidine (note no mutation) Serine Histidine Aspartate Glutamate It was also noticed that a coenzyme molecule containing a hydroxyl (-OH) group binds to the mutated protein in approximately the same location as the original serine but does not alter the structure of the protein in any way. Based on your knowledge of amino acids, enzymes, and catalysis, which of the following is a REASONABLE conclusion? The mutant protein cleaves on the carboxy side of phenylalanine. b. The mutant protein cleaves peptide bonds on the carboxy side of glutamate or aspartate. The mutant protein cleaves peptide bonds on the carboxy side of lysine or arginine. d. The mutant protein functions identical to chymotrypsin. a. C.