Characterization and role of a metalloprotease induced by chitin in Serratia sp. KCK.
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.
Department of Environmental Microbiology, The Helmholtz Center for Infection Research, Braunschweig, Germany. hyun1006@korea.ac.kr
Hyun-Soo
HS
Kim
Peter N
PN
Golyshin
Kenneth N
KN
Timmis
D000595:Amino Acid Sequence; D002686:Chitin / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry; D045726:Metalloproteases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D020539:Sequence Analysis, Protein; D012705:Serratia / Q000187:drug effects* / Q000201:enzymology / Q000235:genetics; D013696:Temperature
D002686:Chitin; D045726:Metalloproteases