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Literature summary extracted from

  • Hysmith, R.M.; Boor, P.J.
    Purification of benzylamine oxidase from cultured porcine aortic smooth muscle cells (1988), Biochem. Cell Biol., 66, 821-829.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.21 Cuprizone
-
 Sus scrofa
1.4.3.21 diethyldithiocarbamate no inhibition Sus scrofa
1.4.3.21 p-chloromercuriphenylsulfonate 0.1 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells Sus scrofa
1.4.3.21 Phenelzine 0.001 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells Sus scrofa
1.4.3.21 Semicarbazide 0.01 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.21 0.0051
-
 benzylamine enzyme from cultured aortic smooth muscle cells, Km decreases with increasing pH Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.21 130000
-
 x * 130000, SDS-PAGE Sus scrofa

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.21
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.3.21 2.08
-
 enzyme from cultured aortic smooth muscle cells Sus scrofa

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.4.3.21 ? x * 130000, SDS-PAGE Sus scrofa