Premium
Amino acid sequence of the chymotryptic protease II from the larvae of the hornet, Vespa crabro
Author(s) -
Jany Klaus-Dieter,
Haug Harald
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80684-x
Subject(s) - chymotrypsin , trypsin , biochemistry , protease , peptide sequence , serine , lysine , elastase , biology , endopeptidase , chemistry , stereochemistry , amino acid , enzyme , gene
The covalent structure of the chymotrypsin II from the larvae of the hornet, Vespa crabro , has been determined. The sequence has been deduced from 3 sets of overlapping peptides generated by trypsin after modification of the lysine or arginine residues and by chymotrypsin. The enzyme is a serine endopeptidase and contains 218 residues in a single polypeptide chain cross‐linked by 3 disulfide bonds. Alignment of the sequence of this insect protease with those of chymotrypsin, elastase and trypsin shows about 35% identity with each and a homologous relationship is evident.