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Peptidyl-Lys metalloendopeptidase

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Peptidyl-Lys metalloendopeptidase
Identifiers
EC no.3.4.24.20
CAS no.65979-41-1
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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

  1. 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.
  2. 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.

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Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins
Matrix metalloproteinases
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