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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Engineering
Engineering on EC 3.4.24.25 - vibriolysin
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additional information
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
additional information
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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