| 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 enzyme is isolated from the honey fungus Armillaria mellea.
- ^ 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.
- Peptidyl-Lys+metalloendopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| 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 enzyme is isolated from the honey fungus Armillaria mellea.
- ^ 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.
- Peptidyl-Lys+metalloendopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)