Peptidyl-Lys metalloendopeptidase
| Peptidyl-Lys metalloendopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.20 | ||||||||
| CAS no. | 65979-41-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Peptidyl-Lys metalloendopeptidase (EC 3.4.24.20, Armillaria mellea neutral proteinase, peptidyllysine metalloproteinase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Preferential cleavage in proteins: -Xaa-Lys- (in which Xaa may be Pro)
This encyme is isolated from the honey fungus Armillaria mellea.
References
- ^ Doonan S, Doonan HJ, Hanford R, Vernon CA, Walker JM, da Airold LP, Bossa F, Barra D, Carloni M, Fasella P, Riva F (1975). "The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues". Biochem. J. 149: 497–506. PMID 1239277.
- ^ Lewis, W.G.; Basford, J.M.; Walton, P.L. (1978). "Specificity and inhibition studies of Armillaria mellea protease". Biochim. Biophys. Acta. 522: 551–560. doi:10.1016/0005-2744(78)90087-6. PMID 23849.
External links
- Peptidyl-Lys+metalloendopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)