Characterization and role of a metalloprotease induced by chitin in Serratia sp. KCK.
dc.contributor.author | Kim, Hyun-Soo | |
dc.contributor.author | Golyshin, Peter N | |
dc.contributor.author | Timmis, Kenneth N | |
dc.date.accessioned | 2008-03-04T15:10:31Z | |
dc.date.available | 2008-03-04T15:10:31Z | |
dc.date.issued | 2007-11 | |
dc.identifier.citation | Characterization and role of a metalloprotease induced by chitin in Serratia sp. KCK. 2007, 34 (11):715-21 J. Ind. Microbiol. Biotechnol. | en |
dc.identifier.issn | 1367-5435 | |
dc.identifier.pmid | 17668255 | |
dc.identifier.doi | 10.1007/s10295-007-0245-1 | |
dc.identifier.uri | http://hdl.handle.net/10033/19693 | |
dc.description.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. | |
dc.language.iso | en | en |
dc.title | Characterization and role of a metalloprotease induced by chitin in Serratia sp. KCK. | en |
dc.type | Article | en |
dc.contributor.department | Department of Environmental Microbiology, The Helmholtz Center for Infection Research, Braunschweig, Germany. hyun1006@korea.ac.kr | en |
dc.identifier.journal | Journal of industrial microbiology & biotechnology | en |
refterms.dateFOA | 2018-06-12T21:30:19Z | |
html.description.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. |