Peptidyl-Lys metalloendopeptidase explained

Peptidyl-Lys metalloendopeptidase
Ec Number:	3.4.24.20
Cas Number:	65979-41-1

Peptidyl-Lys metalloendopeptidase (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.

Notes and 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 . 6 . 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 . 1239277 . 1165654 . 10.1042/bj1490497d .
2. Lewis WG, Basford JM, Walton PL . Specificity and inhibition studies of Armillaria mellea protease . Biochimica et Biophysica Acta (BBA) - Enzymology . 522 . 2 . 551–560 . February 1978 . 23849 . 10.1016/0005-2744(78)90087-6 .