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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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.25 vibriolysin

Cloned

Cloned on EC 3.4.24.25 - vibriolysin

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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
-
expression in Escherichia coli
expression of pro-vibriolysin in Escherichia coli and cleavage of the N-terminal propeptide
-