3.4.24.25: vibriolysin
This is an abbreviated version!
For detailed information about vibriolysin, go to the full flat file.
Word Map on EC 3.4.24.25
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3.4.24.25
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3.4.24.4
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thermolysin
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cholerae
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thermoproteolyticus
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metalloendopeptidase
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proteolyticus
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thermolysin-like
- 3.4.24.25
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3.4.24.4
- thermolysin
- cholerae
- thermoproteolyticus
- metalloendopeptidase
- proteolyticus
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thermolysin-like
Reaction
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
Aeromonas neutral protease, Aeromonas proteolytica neutral proteinase, Aeromonolysin, E495, EC 3.4.24.4, HA/protease, hAPA, hemagglutinin/protease HA/P, MCP-02, MvP1, NprV-R, Proteinase, Aeromonas proteolytica neutral, Vibriolysin
ECTree
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Subunits
Subunits on EC 3.4.24.25 - vibriolysin
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x * 45000, pro-vibriolysin, SDS-PAGE, x * 35000, vibriolysin, SDS-PAGE
monomer
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1 * 35000 (about), Aeromonas proteolytica, sedimentation equilibrium in presence of guanidine-HCl
additional information
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
additional information
gene encodes a signal sequence, an N-terminal propeptide, a mature peptidase domain and a C-terminal propeptide
additional information
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gene encodes a signal sequence, an N-terminal propeptide, a mature peptidase domain and a C-terminal propeptide
additional information
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alpha and beta secondary structure analysis, circular dichroism, overview