ArticleJournal of industrial microbiology & biotechnology2007
Characterization and role of a metalloprotease induced by chitin in Serratia sp. KCK.
Article in Journal of industrial microbiology & biotechnology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- A Bait-and-Switch Strategy Links Phenotypes to Genes Coding for Polymer-Degrading Enzymes in Intact Microbiomes.Microbial biotechnology · 2026Article
- Bioconjugation of Serratiopeptidase with Titanium Oxide Nanoparticles: Improving Stability and Antibacterial Properties.Journal of functional biomaterials · 2024Article
- Understanding pine wilt disease: roles of the pine endophytic bacteria and of the bacteria carried by the disease-causing pinewood nematode.MicrobiologyOpen · 2017Review
- Response Mechanisms in Serratia marcescens IBBCurrent microbiology · 2016Article
- Organic solvent tolerant metallo protease of novel isolate Serratia marcescens PPB-26: production and characterization.3 Biotech · 2016Article
- Nematicidal bacteria associated to pinewood nematode produce extracellular proteases.PloS one · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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