J. Biol. Chem., Vol. 262, Issue 16, 7546-7551, 06, 1987
Complete amino acid sequence of the collagenase from the insect Hypoderma lineatum
A Lecroisey, AM Gilles, A De Wolf and B Keil
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.
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