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