Peptidyl-Lys metalloendopeptidase
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. and 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.
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