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Literature summary extracted from

  • Stesina, L.N.; Akopyan, Z.I.; Gorkin, V.Z.
    Modification of catalytic properties of amine oxidases (1971), FEBS Lett., 16, 349-351.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.22 Sus scrofa
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.22 kidney cortex Sus scrofa
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Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.3.22 0.046
-
 oxidation of histamine, H2S treated enzyme Sus scrofa
1.4.3.22 0.054
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 oxidation of tyramine, H2S treated enzyme Sus scrofa
1.4.3.22 0.058
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 oxidation of serotonine creatine sulfate, H2S treated enzyme Sus scrofa
1.4.3.22 0.11
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 oxidation of tryptamine, H2S treated enzyme Sus scrofa
1.4.3.22 0.13
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 oxidation of putrescine, H2S treated enzyme Sus scrofa
1.4.3.22 0.21
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 oxidation of cadeverine, H2S treated enzyme Sus scrofa
1.4.3.22 0.216
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 oxidation of N-methyl-beta-phenylethylamine, H2S treated enzyme Sus scrofa
1.4.3.22 0.31
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 oxidation of histamine Sus scrofa
1.4.3.22 0.38
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 oxidation of putrescine Sus scrofa
1.4.3.22 0.51
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 oxidation of cadeverine Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.22 RCH2NH2 + H2O + O2 treatment of diamine oxidase with reducing agents induces ability to catalyze oxidative deamination of substrates of monoamine oxidase EC 1.4.3.4 Sus scrofa RCHO + NH3 + H2O2
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