A serine protease uses a serine side chain as a catalytic nucleophile in peptide-bond hydrolysis. In the chymotrypsin family, a catalytic arrangement involving serine, histidine and aspartate promotes formation and hydrolysis of a covalent acyl-enzyme intermediate. The catalytic mechanism and substrate-recognition pocket are distinct: related serine proteases can prefer different cleavage sites. [ref]
New to topics? Read the docs here!