The amino acid sequences around the reactive serine and histidine residues of the chymotrypsin-like protease from the hornet, Vespa orientalis

Abstract

The endopeptidase II from the larva of the hornet Vespa orientalis was inactivated by radioactively labeled active-site-directed inhibitors and afterwards digested with trypsin and chymotrypsin. The labeled peptides were isolated and sequenced. The peptide around the reactive serine residue contains 39 amino acids, and 30 amino acids constitute the peptide around the essential histidine residue. These peptides show sequence homology to the corresponding ones of the trypsin-related endopeptidases.