L-peptidase
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| L-peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.22.46 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
L-peptidase (EC 3.4.22.46) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-Gly bond. Subsequently, it cleaves host cell initiation factor eIF-4G at bonds -Gly-Arg- and -Lys-Arg-
This enzyme is coded bz foot-and-mouth disease virus.
References
- ^ Piccone ME, Zellner M, Kumosinski TF, Mason PW, Grubman MJ (August 1995). "Identification of the active-site residues of the L proteinase of foot-and-mouth disease virus". Journal of Virology. 69 (8): 4950–6. PMC 189310. PMID 7609064.
- ^ Guarné A, Hampoelz B, Glaser W, Carpena X, Tormo J, Fita I, Skern T (October 2000). "Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes". Journal of Molecular Biology. 302 (5): 1227–40. doi:10.1006/jmbi.2000.4115. hdl:10261/111148. PMID 11183785.
External links
- L-peptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
