Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favoured residue, which distinguished this enzyme from thermolysin
Synonyms
vibriolysin, ha/protease, mcp-02, aeromonas neutral protease, more
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favoured residue, which distinguished this enzyme from thermolysin
isolated proteinase MvP1 is non-lethal to salmon at concentrations up to 0.22 microg/g fish. It causes considerable tissue necrosis and hemorrhages at the site of injection, and affects cell-cell adhesions in EPC and BF-2 cell lines, but is not highly cytotoxic. The peptidase partially degrades fish IgM heavy chain but is non-hemolytic
isolated proteinase MvP1 is non-lethal to salmon at concentrations up to 0.22 microg/g fish. It causes considerable tissue necrosis and hemorrhages at the site of injection, and affects cell-cell adhesions in EPC and BF-2 cell lines, but is not highly cytotoxic. The peptidase partially degrades fish IgM heavy chain but is non-hemolytic
treatment of Salmo salar macrophage-like cell line SHK-1 cell with peptidase MvP1 does not cause cell death. In SHK-1 cells, isolated MvP1 peptidase stimulates both interleukin 1beta and interleukin 8 expression
treatment of Salmo salar macrophage-like cell line SHK-1 cell with peptidase MvP1 does not cause cell death. In SHK-1 cells, isolated MvP1 peptidase stimulates both interleukin 1beta and interleukin 8 expression
preference for bonds of the type X-Phe, X-Leu, X-Tyr to which a hydrophobic residue contributes the amino group, and whereas it is essential that the NH2-terminal position of dipeptide substrates be blocked, the enzyme hydrolyzes substrates with free carboxyl groups
isolated proteinase MvP1 is non-lethal to salmon at concentrations up to 0.22 microg/g fish. It causes considerable tissue necrosis and hemorrhages at the site of injection, and affects cell-cell adhesions in EPC and BF-2 cell lines, but is not highly cytotoxic. The peptidase partially degrades fish IgM heavy chain but is non-hemolytic
isolated proteinase MvP1 is non-lethal to salmon at concentrations up to 0.22 microg/g fish. It causes considerable tissue necrosis and hemorrhages at the site of injection, and affects cell-cell adhesions in EPC and BF-2 cell lines, but is not highly cytotoxic. The peptidase partially degrades fish IgM heavy chain but is non-hemolytic
treatment of Salmo salar macrophage-like cell line SHK-1 cell with peptidase MvP1 does not cause cell death. In SHK-1 cells, isolated MvP1 peptidase stimulates both interleukin 1beta and interleukin 8 expression
treatment of Salmo salar macrophage-like cell line SHK-1 cell with peptidase MvP1 does not cause cell death. In SHK-1 cells, isolated MvP1 peptidase stimulates both interleukin 1beta and interleukin 8 expression
Treatment of an encephalitogenic peptide from guinea pig myelin basic protein with alpha-protease and thermolysin. Isolation of fragments and determination of cleavage sites.
Synthesis and HPLC analysis of enzymatically cleavable linker consisting of poly(ethylene glycol) and dipeptide for the development of immunoconjugate.
secretion of HA/protease into the extracellular medium is a two stage process. First, the preproprotein or primary translation product is translocated through the cytoplasmic membrane with removal of its signal peptide by a Sec-dependent mechanism. Second, the proprotein folds in the periplasmic space and is secreted across the outer membrane via the type II secretion system, a multiprotein complex encoded by 12 eps (extracellular protein secretion) genes
secretion of HA/protease into the extracellular medium is a two stage process. First, the preproprotein or primary translation product is translocated through the cytoplasmic membrane with removal of its signal peptide by a Sec-dependent mechanism. Second, the proprotein folds in the periplasmic space and is secreted across the outer membrane via the type II secretion system, a multiprotein complex encoded by 12 eps (extracellular protein secretion) genes
the enzyme exhibits a broad range of potentially pathogenic activities in cell culture and animal models. The activities include the covalent modification of other toxins, the degradation of the protective mucus barrier and disruption of intestinal tight junctions
comparative sequence-structure analysis and molecular dynamics simulations to reveal the molecula features of cold adaptation of enzyme. Enzyme has fewer arginines, a lower Arg/(Lys+Arg) ratio, a lower fraction of large aliphatic residues, more methionines, more serines, and more of the thermolabile amino acid asparagine than other thermolysin enzymes. Additionally, the enzyme has fewer intramolecular cation-pi electron interactions and fewer hydrogen bonds than its pseudolysin or thermolysin counterparts
the MvP1 propeptide undergoes both N-terminal and C-terminal processing and different C-terminal processing results in the formation of several active isoforms of the mature peptidase
secretion of HA/protease into the extracellular medium is a two stage process. First, the preproprotein or primary translation product is translocated through the cytoplasmic membrane with removal of its signal peptide by a Sec-dependent mechanism. Second, the proprotein folds in the periplasmic space and is secreted across the outer membrane via the type II secretion system, a multiprotein complex encoded by 12 eps (extracellular protein secretion) genes. Removal of the HA/protease propeptide and C-terminal processing is presumed to occur in the extracellular medium through an autocatalytic mechanism
isolation of a vibriolysin mutant by in vivo random mutagenensis. contrary to wild-type, the mutant is expressed as active mature vibriolysin in Escherichia coli. The N-terminal propeptide of the engineered enzyme is processed and degraded, confirming that the propeptide inhibits the mature enzyme. Two mutations result in the substitution of stop codon for Trp at position 11 in the signal peptide and of Val for Ala at position 183 in the N-terminal propeptide
isolation of a vibriolysin mutant by in vivo random mutagenensis. contrary to wild-type, the mutant is expressed as active mature vibriolysin in Escherichia coli. The N-terminal propeptide of the engineered enzyme is processed and degraded, confirming that the propeptide inhibits the mature enzyme. Two mutations result in the substitution of stop codon for Trp at position 11 in the signal peptide and of Val for Ala at position 183 in the N-terminal propeptide
expressed in Escherichia coli BL21(DE3) cells. Vibriolysin is not expressed as an active form in Escherichia coli because of the strong inhibitory effect of its N-terminal propeptide. The vibriolysin NprV-R is expressed extracellularly as an active form in Escherichia coli
Cold adaptation of zinc metalloproteases in the thermolysin family from deep sea and arctic sea ice bacteria revealed by catalytic and structural properties and molecular dynamics: new insights into relationship between conformational flexibility and hydr