EC 188.8.131.52 - Vibriolysin
IntEnz Enzyme Nomenclature
- Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favored residue, which distinguished this enzyme from thermolysin.
Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica). Specificity related to, but distinct from, those of thermolysin and bacillolysin . A zinc metallopeptidase in family M4 (thermolysin family). Formerly included in EC 184.108.40.206.
Links to other databases
Esterase activity of zinc neutral proteases.Biochemistry 15: 101-107 (1976). [PMID: 2276]
Aeromonas neutral protease.Methods Enzymol. 45: 404-415 (1976). [PMID: 1012006]
Aeromonas neutral protease: specificity toward extended substrates.Arch. Biochem. Biophys. 204: 214-219 (1980). [PMID: 7000005]
Critical ionizing groups in Aeromonas neutral protease.J. Biol. Chem. 263: 1821-1825 (1988). [PMID: 3123480]
Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus.Gene 112: 107-112 (1992). [PMID: 12022200]
[EC 220.127.116.11 created 1972 as EC 18.104.22.168, part transferred 1992 to EC 22.214.171.124, modified 1997]