Vibriolysin

Vibriolysin
Identifiers
EC number	3.4.24.25
CAS number	69598-88-5
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

Vibriolysin (EC 3.4.24.25, Aeromonas proteolytica neutral proteinase, aeromonolysin) is an enzyme.^{[1][2][3][4][5]} This enzyme catalyses the following chemical 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

This thermostable enzyme is isolated from Vibrio proteolyticus.

References

1. Holmquist, B. and Vallee, B.L. (1976). "Esterase activity of zinc neutral proteases". Biochemistry 15: 101–107. doi:10.1021/bi00646a016. PMID 2276.
2. Wilkes, S.H. and Prescott, J.M. (1976). "Aeromonas neutral protease". Methods Enzymol. 45: 404–415. doi:10.1016/s0076-6879(76)45036-x. PMID 1012006.
3. Bayliss, M.E., Wilkes, S.H. and Prescott, J.M. (1980). "Aeromonas neutral protease: specificity toward extended substrates". Arch. Biochem. Biophys. 204: 214–219. doi:10.1016/0003-9861(80)90026-0. PMID 7000005.
4. Wilkes, S.H., Bayliss, M.E. and Prescott, J.M. (1988). "Critical ionizing groups in Aeromonas neutral protease". J. Biol. Chem. 263: 1821–1825. PMID 3123480.
5. David, V.A., Deutch, A.H., Sloma, A., Pawlyk, D., Ally, A. and Durham, D.R. (1992). "Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus". Gene 112: 107–112. doi:10.1016/0378-1119(92)90310-l. PMID 1551587.

External links

• Vibriolysin at the US National Library of Medicine Medical Subject Headings (MeSH)