Open AccessThe 105‐kDa protein component of Bacillus cereus non‐haemolytic enterotoxin (Nhe) is a metalloprotease with gelatinolytic and collagenolytic activity
Author(s) -
Lund Terje,
Granum Per Einar
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb08699.x
Subject(s) - bacillus cereus , collagenase , enterotoxin , clostridium perfringens , thermolysin , biochemistry , metalloproteinase , gelatinase , proteolysis , chemistry , microbiology and biotechnology , peptide sequence , biology , bacteria , enzyme , escherichia coli , trypsin , gene , genetics
A sequence of 91 amino acids residues, probably starting from the N‐terminal of the mature protein, was determined for the 105‐kDa protein of the non‐haemolytic enterotoxin of Bacillus cereus . The last part of this sequence was similar to parts of the N‐terminal portions of two collagenases of Clostridium histolyticum and Clostridium perfringens . Zymography, with intact collagen fibril and gelatin as substrates, showed that the 105‐kDa protein had collagenolytic and gelatinolytic activity. The 105‐kDa protein also showed activity against a typical collagenase substrate, azocoll, and was inhibited by EDTA and 1,10‐phenanthroline. We conclude that the 105‐kDa protein is a collagenase.