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Literature summary for 1.4.3.21 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
Search for more literature for 1.4.3.21

Inhibitors

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
 Sus scrofa
-

Substrates and Products (Substrate)

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

Subunits

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

Ki Value [mM]

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