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Literature summary extracted from

  • Barker, R.; Boden, N.; Cayley, G.; Charlton, S.C.; Henson, R.; Holmes, M.C.; Kelly, I.D.; Knowles, P.F.
    Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods (1979), Biochem. J., 177, 289-302.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.21 azide
-
Sus scrofa
1.4.3.21 cyanide uncompetitive vs. benzylamine, non-competititve vs. O2 Sus scrofa
1.4.3.21 NaN3 azide binds to Cu2+ ions, competitive inhibition vs. O2, uncompetitive vs. benzylamine Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.3.21 copper study of cupric ions by magnetic-resonance and kinetic methods, native enzyme contains 2 tightly bound Cu2+ ions Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.21 97000
-
2 * 97000, SDS-PAGE Sus scrofa
1.4.3.21 186000
-
sedimentation-equilibrium Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.21 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.21 blood plasma
-
Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.21 RCH2NH2 + H2O + O2
-
Sus scrofa RCHO + NH3 + H2O2
-
?

Subunits

EC Number Subunits Comment Organism
1.4.3.21 dimer 2 * 97000, SDS-PAGE Sus scrofa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.4.3.21 0.76
-
cyanide vs. O2, deduced from slope Sus scrofa
1.4.3.21 2.17
-
cyanide vs. benzylamine Sus scrofa
1.4.3.21 2.9
-
cyanide vs. O2, deduced from intercept Sus scrofa
1.4.3.21 40
-
azide vs. benzylamine Sus scrofa
1.4.3.21 84
-
azide vs. O2 Sus scrofa