Abstract
The properties of a derivative of α-chymotrypsin in which histidine-57 has been methylated have been examined. Although the modified enzyme binds substrate with the same affinity as does native α-chymotrypsin, acylation and deacylation occur at much decreased rates. As for native α-chymotrypsin, a basic group of pKa approx. 7 is involved in both acylation and deacylation. The significance of these results is considered in relation to the normal function of histidine-57.