<prompt> If chymotrypsin molecule undergoes a ser-195-ala mutation then -Chymotrypsin will not bind the substrateChymotrypsin will bind the substrate as well as cause cleavageChymotrypsin will bind the substrate but will not cause cleavageNo affect will be observed  <response>: The substrate binds but does not cleave Serine-195 is involved in catalytic activity but not in binding.Serine-195 is the highly reactive residue of chymotrypsin.The peptide bond is hydrolyzed through the acid-catalyzed nucleophilic attack, utilizing the serine 195 residue of the enzyme.The enzyme-substrate complex is formed by the binding of the aromatic amino acid residue with the hydrophilic pocket on the active site of the enzyme ser-195 has no role in binding.Binding of substrate initiates proton shifts that in effect transfer the hydroxyl proton of ser 195 to Asp 102. This results in the formation of a covalent acyl-enzyme intermediate.Further proton on Asp 102 then shuttles through His 57 to the amino group and the peptide bond is cleaved.Thus, Asp 102-His 57-ser 195 constitute a charge-relay network that functions as a proton shuttle. 