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Literature summary extracted from

  • Oreland, L.
    Purification and properties of pig liver mitochondrial monoamine oxidase (1971), Arch. Biochem. Biophys., 146, 410-412.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.4 additional information
-
additional information Km of membrane-bound and Triton X-100-solubilized enzyme Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.3.4 mitochondrion
-
Sus scrofa 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.3.4 Cu2+ negligible amounts in the purified enzym Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.4 115000
-
gel filtration, lowest molecular weight determined, variations due to different states of aggregation Sus scrofa

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.4.3.4 additional information when enzyme liberated by methyl ethyl ketone extraction Km about 3times lower than that for enzyme bound to the mitochondria or solubilzed by Triton X-100 Sus scrofa

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.4.3.4 additional information enzyme is bound to the mitochondria by acidic phospholipids, soluble enzyme can form complexes with such phospholipids Sus scrofa

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.4
-
Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.4 liver
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.3.4 additional information
-
-
Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.4 benzylamine + H2O + O2
-
Sus scrofa benzaldehyde + NH3 + H2O2
-
?
1.4.3.4 kynuramine + H2O + O2
-
Sus scrofa 3-(2-aminophenyl)-3-oxopropanal + NH3 + H2O2
-
?
1.4.3.4 RCH2NH2 + H2O + O2 no activity with spermidine Sus scrofa RCHO + NH3 + H2O2
-
?
1.4.3.4 RCH2NH2 + H2O + O2 no activity with histamine Sus scrofa RCHO + NH3 + H2O2
-
?
1.4.3.4 RCH2NH2 + H2O + O2 no activity with spermine Sus scrofa RCHO + NH3 + H2O2
-
?
1.4.3.4 RCH2NH2 + H2O + O2 phenylethylhydrazine Sus scrofa RCHO + NH3 + H2O2
-
?
1.4.3.4 RCH2NH2 + H2O + O2 isoamylamine Sus scrofa RCHO + NH3 + H2O2
-
?
1.4.3.4 RCH2NH2 + H2O + O2 3-hydroxytyramine Sus scrofa RCHO + NH3 + H2O2
-
?
1.4.3.4 RCH2NH2 + H2O + O2 amylamine Sus scrofa RCHO + NH3 + H2O2
-
?
1.4.3.4 serotonin + H2O + O2
-
Sus scrofa (5-hydroxy-1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
?
1.4.3.4 tryptamine + H2O + O2
-
Sus scrofa 1H-indol-3-yl-acetaldehyde + NH3 + H2O2
-
?
1.4.3.4 tyramine + H2O + O2
-
Sus scrofa (4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.4 8.7
-
tyramine as substrate Sus scrofa
1.4.3.4 9.2
-
benzylamine as substrate Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.4.3.4 7 11 about 50% of activity maximum at pH 7 and 11 Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.4 flavin flavoprotein Sus scrofa
1.4.3.4 flavin 1 mol FAD per 115000 g of protein Sus scrofa