V-cath endopeptidase
| V-cath endopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.22.50 | ||||||||
| CAS no. | 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[edit]
- ^ Slack JM, Kuzio J, Faulkner P (May 1995). "Characterization of v-cath, a cathepsin L-like proteinase expressed by the baculovirus Autographa californica multiple nuclear polyhedrosis virus". The Journal of General Virology. 76 ( Pt 5) (5): 1091–8. doi:10.1099/0022-1317-76-5-1091. PMID 7730794.
- ^ Hawtin RE, Zarkowska T, Arnold K, Thomas CJ, Gooday GW, King LA, Kuzio JA, Possee RD (November 1997). "Liquefaction of Autographa californica nucleopolyhedrovirus-infected insects is dependent on the integrity of virus-encoded chitinase and cathepsin genes". Virology. 238 (2): 243–53. doi:10.1006/viro.1997.8816. PMID 9400597.
External links[edit]
- V-cath+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
