Vibriolysin
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
| 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 | ||||||||
| |||||||||
This thermostable enzyme is isolated from Vibrio proteolyticus.
References
- Holmquist B, Vallee BL (January 1976). "Esterase activity of zinc neutral proteases". Biochemistry. 15 (1): 101–7. doi:10.1021/bi00646a016. PMID 2276.
- Wilkes SH, Prescott JM (1976). "Aeromonas neutral protease". Methods in Enzymology. 45: 404–15. doi:10.1016/s0076-6879(76)45036-x. PMID 1012006.
- Bayliss ME, Wilkes SH, Prescott JM (October 1980). "Aeromonas neutral protease: specificity toward extended substrates". Archives of Biochemistry and Biophysics. 204 (1): 214–9. doi:10.1016/0003-9861(80)90026-0. PMID 7000005.
- Wilkes SH, Bayliss ME, Prescott JM (February 1988). "Critical ionizing groups in Aeromonas neutral protease". The Journal of Biological Chemistry. 263 (4): 1821–5. PMID 3123480.
- David VA, Deutch AH, Sloma A, Pawlyk D, Ally A, Durham DR (March 1992). "Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus". Gene. 112 (1): 107–12. doi:10.1016/0378-1119(92)90310-l. PMID 1551587.
External links
- Vibriolysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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