2.50
Hdl Handle:
http://hdl.handle.net/10033/19693
Title:
Characterization and role of a metalloprotease induced by chitin in Serratia sp. KCK.
Authors:
Kim, Hyun-Soo; Golyshin, Peter N; Timmis, Kenneth N
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.
Affiliation:
Department of Environmental Microbiology, The Helmholtz Center for Infection Research, Braunschweig, Germany. hyun1006@korea.ac.kr
Citation:
Characterization and role of a metalloprotease induced by chitin in Serratia sp. KCK. 2007, 34 (11):715-21 J. Ind. Microbiol. Biotechnol.
Journal:
Journal of industrial microbiology & biotechnology
Issue Date:
Nov-2007
URI:
http://hdl.handle.net/10033/19693
DOI:
10.1007/s10295-007-0245-1
PubMed ID:
17668255
Type:
Article
Language:
en
ISSN:
1367-5435
Appears in Collections:
Publications of RG Environmental Microbiology (UMW)

Full metadata record

DC FieldValue Language
dc.contributor.authorKim, Hyun-Soo-
dc.contributor.authorGolyshin, Peter N-
dc.contributor.authorTimmis, Kenneth N-
dc.date.accessioned2008-03-04T15:10:31Z-
dc.date.available2008-03-04T15:10:31Z-
dc.date.issued2007-11-
dc.identifier.citationCharacterization and role of a metalloprotease induced by chitin in Serratia sp. KCK. 2007, 34 (11):715-21 J. Ind. Microbiol. Biotechnol.en
dc.identifier.issn1367-5435-
dc.identifier.pmid17668255-
dc.identifier.doi10.1007/s10295-007-0245-1-
dc.identifier.urihttp://hdl.handle.net/10033/19693-
dc.description.abstractA 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.en
dc.language.isoenen
dc.titleCharacterization and role of a metalloprotease induced by chitin in Serratia sp. KCK.en
dc.typeArticleen
dc.contributor.departmentDepartment of Environmental Microbiology, The Helmholtz Center for Infection Research, Braunschweig, Germany. hyun1006@korea.ac.kren
dc.identifier.journalJournal of industrial microbiology & biotechnologyen

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