Proteolytic enzymes: lipophilic binding sites for specific and non-specific substrates of α-chymotrypsin
Abstract
Evidence is presented consistent with a lipophilic binding site for the leaving group and for the alkyl or aromatic function of the acylamino-group in specific substrates of α-chymotrypsin. Binding of small, non-specific substrates and inhibitors to α-chymotrypsin is shown, by comparison with elastase, to involve at the most only a small fraction of the ‘ tosyl-hole. ’