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Literature summary for 1.4.3.21 extracted from

  • Falk, M.C.; Staton, A.J.; Williams, T.J.
    Heterogeneity of pig plasma amine oxidase: molecular and catalytic properties of chromatographically isolated forms (1983), Biochemistry, 22, 3746-3751.
    View publication on PubMed
Search for more literature for 1.4.3.21

Inhibitors

Inhibitors Comment Organism Structure
phenylhydrazine
-
 Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.075 0.095 benzylamine
-
 Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
copper 2 mol of Cu2+ per dimer Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
95000
-
 2 * 95000, SDS-PAGE Sus scrofa
196000
-
 gradient PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein heterogenity of pig plasma amine oxidase may be due to variable carbohydrate content Sus scrofa

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.105
-
-
 Sus scrofa

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 95000, SDS-PAGE Sus scrofa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
188 198 benzylamine
-
 Sus scrofa

Cofactor

Cofactor Comment Organism Structure
additional information contains one "active-carbonyl" cofactor per dimer Sus scrofa