Peptidyl-Lys metalloendopeptidase

Peptidyl-Lys metalloendopeptidase
Identifiers
EC number 3.4.24.20
CAS number 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 encyme is isolated from the honey fungus Armillaria mellea.

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 (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.
  2. Lewis, W.G.; Basford, J.M.; 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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