Amino acid sequence of an insect chymotrypsin from the larvae of the hornet, Vespa orientalis.
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.
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*
D010446:Peptide Fragments; D010450:Endopeptidases; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin