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Literature summary for 1.4.3.21 extracted from

  • Klema, V.J.; Solheid, C.J.; Klinman, J.P.; Wilmot, C.M.
    Structural analysis of aliphatic versus aromatic substrate specificity in a copper amine oxidase from Hansenula polymorpha (2013), Biochemistry, 52, 2291-2301.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Saccharomyces cerevisiae Ogataea angusta

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with ethylamine and benzylamine, hanging drop vapor diffusion method, using 8-9% (w/v) polyethylene glycol 8000 in 0.22-0.25 M potassium phosphate (pH 6.0) Ogataea angusta

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Ogataea angusta the catalytic mechanism can be divided into two half-reactions: a reductive half-reaction in which a primary amine substrate is oxidized to its corresponding aldehyde with the concomitant reduction of the organic cofactor 2,4,5-trihydroxyphenylalanine quinone and an oxidative half-reaction in which reduced 2,4,5-trihydroxyphenylalanine quinone is re-oxidized with the reduction of molecular oxygen to hydrogen peroxide ?
-
?

Organism

Organism UniProt Comment Textmining
Ogataea angusta P12807
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Ogataea angusta

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzylamine + H2O + O2
-
Ogataea angusta benzaldehyde + NH3 + H2O2
-
?
ethylamine + H2O + O2
-
Ogataea angusta acetaldehyde + NH3 + H2O2
-
?
additional information the catalytic mechanism can be divided into two half-reactions: a reductive half-reaction in which a primary amine substrate is oxidized to its corresponding aldehyde with the concomitant reduction of the organic cofactor 2,4,5-trihydroxyphenylalanine quinone and an oxidative half-reaction in which reduced 2,4,5-trihydroxyphenylalanine quinone is re-oxidized with the reduction of molecular oxygen to hydrogen peroxide Ogataea angusta ?
-
?

Synonyms

Synonyms Comment Organism
CAO
-
Ogataea angusta
Copper amine oxidase
-
Ogataea angusta
hPAO-1
-
Ogataea angusta

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.066
-
benzylamine in 100 mM potassium phosphate, pH 7.2, temperature not specified in the publication Ogataea angusta
20
-
ethylamine in 100 mM potassium phosphate, pH 7.2, temperature not specified in the publication Ogataea angusta

Cofactor

Cofactor Comment Organism Structure
2,4,5-trihydroxyphenylalanine quinone
-
Ogataea angusta

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.09
-
benzylamine in 100 mM potassium phosphate, pH 7.2, temperature not specified in the publication Ogataea angusta
52
-
ethylamine in 100 mM potassium phosphate, pH 7.2, temperature not specified in the publication Ogataea angusta