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Literature summary for 1.4.3.21 extracted from

  • Stevanato, R.; Cardillo, S.; Braga, M.; De Iuliis, A.; Battaglia, V.; Toninello, A.; Agostinelli, E.; Vianello, F.
    Preliminary kinetic characterization of a copper amine oxidase from rat liver mitochondria matrix (2011), Amino Acids, 40, 713-720.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis at different ionic strength and pH, overview Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Rattus norvegicus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ dependent on Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information docking of substrates to the enzyme, the enzyme shows electrostatic control of the docking process, overview. The active site contains two negatively charged amino acid residues which seem to interact with positively charged groups of the substrate molecules Rattus norvegicus ?
-
?

Synonyms

Synonyms Comment Organism
copper-dependent amine oxidase
-
Rattus norvegicus

pH Range

pH Minimum pH Maximum Comment Organism
5.6 10.2 assay range Rattus norvegicus