V-cath endopeptidase
| V-cath endopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.22.50 | ||||||||
| CAS number | 316365-69-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
V-cath endopeptidase (EC 3.4.22.50, AcNPV protease, BmNPV protease, NPV protease, baculovirus cathepsin, nucleopolyhedrosis virus protease, viral cathepsin) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B
This enzyme belongs to the peptidase family C1.
References
- ↑ Slack, J.M.; Kuzio, J.; Faulkner, P. (1995). "Characterization of V-cath, a cathepsin L-like proteinase expressed by the baculovirus Autographa californica multiple nuclear polyhedrosis-virus". J. Gen. Virol. 76: 1091–1098. doi:10.1099/0022-1317-76-5-1091. PMID 7730794.
- ↑ Hawtin, R.E.; Zarkowska, T.; Arnold, K.; Thomas, C.J.; Gooday, G.W.; King, L.A.; Kuzio, J.A.; Possee, R.D. (1997). "Liquefaction of Autographa californica nucleopolyhedrovirus-infected insects is dependent on the integrity of virus-encoded chitinase and cathepsin genes". Virology. 238: 243–253. doi:10.1006/viro.1997.8816. PMID 9400597.
External links
- V-cath endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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