= Serine protease
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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. <PeptideCutter - Cleavage specificities of selected enzymes and chemicals (ExPASy)>[Chymotrypsin and trypsin cleavage preferences]{ref}
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