3.4.24.25: vibriolysin

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For detailed information about vibriolysin, go to the full flat file.

Word Map on EC 3.4.24.25

3.4.24.25

3.4.24.4

thermolysin

cholerae

thermoproteolyticus

metalloendopeptidase

proteolyticus

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

3 Hydrolases

3.4 Acting on peptide bonds (peptidases)

3.4.24 Metalloendopeptidases

3.4.24.25 vibriolysin

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Results	in table
55	AA Sequence
1	CAS Registry Number
5	Cloned(Commentary)
1	General Information
1	General Stability
20	Inhibitors
2	kcat/KM [mM/s]
11	KM Value [mM]
1	Localization
6	Metals/Ions
4	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
14	Organism
5	PDB ID
3	pH Optimum
1	pH Stability
4	Posttranslational Modification
1	Protein Variants
5	Purification (Commentary)
1	Reaction
1	Reaction Type
14	Reference
2	Source Tissue
3	Specific Activity [micromol/min/mg]
1	Storage Stability
47	Substrates and Products (Substrate)
5	Subunits
14	Synonyms
5	Temperature Optimum [°C]
3	Temperature Range [°C]
4	Temperature Stability [°C]
9	Turnover Number [1/s]

Turnover Number

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Turnover Number on EC 3.4.24.25 - vibriolysin

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2.5

Benzyloxycarbonyl-Gly-Ile-NH2

Vibrio proteolyticus

31111

Benzyloxycarbonyl-Gly-Leu-NH2

Vibrio proteolyticus

31112

Benzyloxycarbonyl-Gly-norvaline-NH2

Vibrio proteolyticus

31111

1150

benzyloxycarbonyl-Gly-Phe-Gly-NH2

Vibrio proteolyticus

31110

0.4 - 584

Benzyloxycarbonyl-Gly-Phe-NH2

2 entries

Benzyloxycarbonyl-Gly-Tyr

Vibrio proteolyticus

31112

0.5

Benzyloxycarbonyl-Gly-Tyr-NH2

Vibrio proteolyticus

31111

additional information

Vibrio proteolyticus

overview: effect of residues at P1', P1'' or P2' on turnover number, influence of the identity of residues remote from scissile bond

31111