ENZYME entry: EC 3.4.22.46
| Accepted Name |
| L-peptidase.
|
| Reaction catalysed |
| Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg- |
| Comment(s) |
- Best known from foot-and-mouth disease virus, but occurs in other
aphthoviruses and cardioviruses.
- Destruction of initiation factor eIF-4G has the effect of shutting
off host-cell protein synthesis while allowing synthesis of viral
proteins to continue.
- The tertiary structure reveals a distant relationship to papain and,
consistent with this, compound E-64 is inhibitory.
- Belongs to peptidase family C28.
|
| Cross-references |
| BRENDA | 3.4.22.46 |
| EC2PDB | 3.4.22.46 |
| ExplorEnz | 3.4.22.46 |
| PRIAM enzyme-specific profiles | 3.4.22.46 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.22.46 |
| IUBMB Enzyme Nomenclature | 3.4.22.46 |
| IntEnz | 3.4.22.46 |
| MEDLINE | Find literature relating to 3.4.22.46 |
| MetaCyc | 3.4.22.46 |
| UniProtKB/Swiss-Prot |
|
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