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)
Peptidyl-Lys metalloendopeptidase
Identifiers
EC number3.4.24.20
CAS number65979-41-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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. PMC 1165654. 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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