Biology:Peptidyl-Lys metalloendopeptidase
From HandWiki
| Peptidyl-Lys metalloendopeptidase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.24.20 | ||||||||
| CAS number | 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 | ||||||||
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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 enzyme is isolated from the honey fungus Armillaria mellea.
References
- ↑ "The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues". The Biochemical Journal 149 (3): 497–506. September 1975. doi:10.1042/bj1490497d. PMID 1239277.
- ↑ "Specificity and inhibition studies of Armillaria mellea protease". Biochimica et Biophysica Acta (BBA) - Enzymology 522 (2): 551–560. February 1978. doi:10.1016/0005-2744(78)90087-6. PMID 23849.
External links
- Peptidyl-Lys+metalloendopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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