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Characterization and role of a metalloprotease induced by chitin in Serratia sp. KCK.

Kim, Hyun-Soo
Golyshin, Peter N
Timmis, Kenneth N
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2007-11
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A metalloprotease induced by chitin in a new chitinolytic bacterium Serratia sp. Strain KCK was purified and characterized. Compared with other Serratia enzymes, it exhibited a rather broad pH activity range (pH 5.0-8.0), and thermostability. The cognate ORF, mpr, was cloned and expressed. Its deduced amino acid sequence showed high similarity to those of bacterial zinc-binding metalloproteases and a well-conserved serralysin family motif. Pretreatment of chitin with the Mpr protein promoted chitin degradation by chitinase A, which suggests that Mpr participates in, and facilitates, chitin degradation by this microorganism.
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Characterization and role of a metalloprotease induced by chitin in Serratia sp. KCK. 2007, 34 (11):715-21 J. Ind. Microbiol. Biotechnol.
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Article
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en
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1367-5435
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