An exocellular thermolysin-like metalloprotease produced by Vibrio fluvialis: purification, characterization, and gene cloning.
An exocellular metalloprotease produced by Vibrio fluvialis, an enteropathogenic vibrio, was purified and characterized. The metalloprotease (V. fluvialis protease [VFP]) was found to have very similar characteristics to V. vulnificus protease, including a molecular mass of 45kDa, sensitivity to chelating agents or competitive inhibitors for thermolysin-like metalloproteases, and the substrate specificity. The structural gene for VFP was also cloned, and its nucleotide sequence was determined. The deduced amino acid sequence confirmed that VFP was a member of the thermolysin family. VFP, like V. vulnificus protease, showed the haemagglutinating, permeability-enhancing and haemorrhagic activities in addition to the proteolytic activity toward oligopeptide, casein or elastin.
Miyoshi
Shin-ichi
S
Faculty of Pharmaceutical Sciences and Okayama University, Tsushima-Naka, Okayama, 700-8530, Japan
Sonoda
Yuka
Y
Wakiyama
Hiroko
H
Rahman
Md Monzur
MM
Tomochika
Ken-ichi
K
Shinoda
Sumio
S
Yamamoto
Shigeo
S
Tobe
Kazuo
K
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D005798:Genes, Bacterial; D008666:Metalloendopeptidases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism; D013820:Thermolysin / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D014733:Vibrio / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D010455:Peptides; D008666:Metalloendopeptidases; C466986:VfpA protein, Vibrio fluvialis; D013820:Thermolysin