| EC |
3.4.24.20 |
| Accepted name: |
peptidyl-Lys metalloendopeptidase |
| Reaction: |
Preferential cleavage in proteins: -Xaa┼Lys- (in which Xaa may be Pro) |
| Other name(s): |
Armillaria mellea neutral proteinase; peptidyllysine metalloproteinase |
| Comments: |
From the honey fungus Armillaria mellea. In peptidase family M35 (deuterolysin family). |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 65979-41-1 |
| References: |
| 1. |
Doonan S, Doonan HJ, Hanford R, Vernon CA, Walker JM, da Airold LP, Bossa F, Barra D, Carloni M, Fasella P, Riva F. The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues. Biochem. J. 149 (1975) 497–506. [PMID: 1239277] |
| 2. |
Lewis, W.G., Basford, J.M. and Walton, P.L. Specificity and inhibition studies of Armillaria mellea protease. Biochim. Biophys. Acta 522 (1978) 551–560. [DOI] [PMID: 23849] |
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| [EC 3.4.24.20 created 1978 as EC 3.4.99.32, transferred 1992 to EC 3.4.24.20 (EC 3.4.99.30 created 1978, incorporated 1992)] |
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