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- W1990168008 abstract "E chrysanthemi, a phytopathogenic enterobacterium, secretes several enzymes into the medium such as pectinases cellulases and proteases. It also produces 3 distinct and antigenically related extracellular proteases. The proteases secretion pathway seems to be distinct from that of the other extracellular enzymes since pleiotropic mutants impaired in cellulase and pectinase are unimpaired in protease secretion. E chrysanthemi proteases B and C secretion occurs without an N-terminal signal peptide and is dependent upon specific secretion functions which are encoded by genes adjacent to the protease structural genes. This secretion pathway might be analogous to the α-hemolysin secretion pathway in E coli. Protection against intracellular proteolytic activity is achieved by 2 distinct mechanisms: the proteases are synthesized as inactive precursors with an N-terminal extension of 15 aminoacids (protease B) and 17 aminoacids (protease C) absent in the mature active extracellular enzymes; an intracellular specific inhibitor is produced by osme E chrysanthemi strains." @default.
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- W1990168008 date "1990-02-01" @default.
- W1990168008 modified "2023-10-07" @default.
- W1990168008 title "Secretion processing and activation of Erwinia chrysanthemi proteases" @default.
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- W1990168008 doi "https://doi.org/10.1016/0300-9084(90)90139-8" @default.
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