| Literature DB >> 17668255 |
Hyun-Soo Kim1, Peter N Golyshin, Kenneth N Timmis.
Abstract
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.Entities:
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Year: 2007 PMID： 17668255 DOI： 10.1007/s10295-007-0245-1
Source DB: PubMed Journal: J Ind Microbiol Biotechnol ISSN： 1367-5435 Impact factor: 3.346