title: Complete amino acid sequence of the collagenase from the insect Hypoderma lineatum.
abstract: The primary structure of the Hypoderma lineatum collagenase was determined. Chymotrypsin digestion and thermolysin fragmentation of the chymotryptic core gave 30 and 5 peptides, respectively, accounting for all the residues of the protein. These peptides were aligned with overlapping peptides derived from tryptic and Staphylococcus aureus V8 proteinase digests. Hypoderma collagenase is a serine proteinase composed of 230 amino acids (Mr 25,223). It displays a high degree of sequential homology with the serine proteinases of the trypsin family, especially with another collagenolytic enzyme, the proteinase I of the crab Uca pugilator. The six half-cystinyl residues of Hypoderma collagenase correspond to 6 of the 10 half-cystinyl residues of chymotrypsin, and the residues forming the charge-relay system of the active site of chymotrypsin (His-57, Asp-102, and Ser-195) are found in corresponding regions. The prediction of the secondary structure of the collagenase is given.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide; D004175:Diptera / Q000201:enzymology*; D003012:Microbial Collagenase; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases
chemical_list: D010446:Peptide Fragments; D010447:Peptide Hydrolases; D003012:Microbial Collagenase; D003488:Cyanogen Bromide