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Literature summary for 1.4.3.22 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
Search for more literature for 1.4.3.22

Organism

Organism UniProt Comment Textmining
Sus scrofa
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Source Tissue

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

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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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