Peptidyl-Lys metalloendopeptidase | |||||||||
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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 | ||||||||
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Peptidyl-Lys metalloendopeptidase (EC 3.4.24.20, Armillaria mellea neutral proteinase, peptidyllysine metalloproteinase) is an enzyme. 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
- Doonan S, Doonan HJ, Hanford R, Vernon CA, Walker JM, da Airold LP, et al. (September 1975). "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. doi:10.1042/bj1490497d. PMC 1165654. PMID 1239277.
- Lewis WG, Basford JM, Walton PL (February 1978). "Specificity and inhibition studies of Armillaria mellea protease". Biochimica et Biophysica Acta (BBA) - Enzymology. 522 (2): 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)
Proteases: metalloendopeptidases (EC 3.4.24) | |
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ADAM proteins | |
Matrix metalloproteinases | |
Other |
Enzymes | |
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