title: Amino acid sequence of an insect chymotrypsin from the larvae of the hornet, Vespa orientalis.
abstract: The complete amino acid sequence of the endopeptidase II from the larvae of the hornet, Vespa orientalis, has been determined. The enzyme is a single polypeptide chain of 216 residues. The protease is a serine endopeptidase. When aligned for optimal homology to the trypsin related proteases, the insect endopeptidase displays 37% identity with bovine chymotrypsin. The structure of the hornet protease is the first reported for a serine endopeptidase from an insect.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002918:Chymotrypsin; D010450:Endopeptidases; D006927:Hymenoptera / Q000201:enzymology*; D007814:Larva / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis; D012697:Serine Endopeptidases; D013329:Structure-Activity Relationship; D014357:Trypsin; D014863:Wasps / Q000201:enzymology*
chemical_list: D010446:Peptide Fragments; D010450:Endopeptidases; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin