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Literature summary for 1.4.3.21 extracted from

  • Dainese, E.; Sabatucci, A.; Pintus, F.; Medda, R.; Angelucci, C.B.; Floris, G.; Maccarrone, M.
    Domain mobility as probed by small-angle X-ray scattering may account for substrate access to the active site of two copper-dependent amine oxidases (2014), Acta Crystallogr. Sect. D, 70, 2101-2110 .
    View publication on PubMed
Search for more literature for 1.4.3.21

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ dependent on Euphorbia characias
Cu2+ dependent on Lens culinaris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
200000
-
 gel filtration Euphorbia characias
200000
-
 gel filtration Lens culinaris

Organism

Organism UniProt Comment Textmining
Euphorbia characias Q9SW90
-
-
Lens culinaris P49252
-
-

Source Tissue

Source Tissue Comment Organism Textmining
latex
-
 Euphorbia characias
-
latex
-
 Lens culinaris
-
seedling
-
 Euphorbia characias
-
seedling
-
 Lens culinaris
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
putrescine + H2O + O2
-
 Euphorbia characias ?
-
 ?
putrescine + H2O + O2
-
 Lens culinaris ?
-
 ?

Synonyms

Synonyms Comment Organism
CAO
-
 Euphorbia characias
CAO
-
 Lens culinaris
copper-dependent amine oxidase
-
 Euphorbia characias
copper-dependent amine oxidase
-
 Lens culinaris
Cu/TPQ amine oxidase
-
 Euphorbia characias
Cu/TPQ amine oxidase
-
 Lens culinaris
quinoprotein copper-containing amine oxidase
-
 Euphorbia characias
quinoprotein copper-containing amine oxidase
-
 Lens culinaris

Cofactor

Cofactor Comment Organism Structure
2,4,5-trihydroxyphenylalanine quinone
-
 Euphorbia characias
2,4,5-trihydroxyphenylalanine quinone
-
 Lens culinaris