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Literature summary extracted from

  • Chang, C.M.; Klema, V.J.; Johnson, B.J.; Mure, M.; Klinman, J.P.; Wilmot, C.M.
    Kinetic and structural analysis of substrate specificity in two copper amine oxidases from Hansenula polymorpha (2010), Biochemistry, 49, 2540-2550.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.21 expressed in Saccharomyces cerevisiae INVSC-1 cells Ogataea angusta

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.3.21 isoform HPAO-2, sitting drop vapor diffusion method, using 0.5-0.75 M potassium sodium tartrate tetrahydrate in 0.10 M phosphate, pH 6.0-7.5, at 20°C Ogataea angusta

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.21 72000
-
 x * 72000, SDS-PAGE Ogataea angusta

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.21 Ogataea angusta P12807
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.21 Q sepharose column chromatography Ogataea angusta

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.21 benzylamine + H2O + O2
-
 Ogataea angusta benzaldehyde + NH3 + H2O2
-
 ?
1.4.3.21 methylamine + H2O + O2
-
 Ogataea angusta formaldehyde + NH3 + H2O2
-
 ?
1.4.3.21 additional information isoform HPAO-2 shows a clear preference for bulkier aromatic amines and isoform HPAO-1 shows a preference for short aliphatic amines Ogataea angusta ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.3.21 ? x * 72000, SDS-PAGE Ogataea angusta

Synonyms

EC Number Synonyms Comment Organism
1.4.3.21 CAO
-
 Ogataea angusta
1.4.3.21 Copper amine oxidase
-
 Ogataea angusta
1.4.3.21 hPAO-1 isoform Ogataea angusta
1.4.3.21 HPAO-2 isoform Ogataea angusta

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.21 0.066
-
 benzylamine isoform HPAO-1, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta
1.4.3.21 2.18
-
 methylamine isoform HPAO-2, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta
1.4.3.21 6.2
-
 methylamine isoform HPAO-1, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta
1.4.3.21 8.1
-
 benzylamine isoform HPAO-2, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.21 2,4,5-trihydroxyphenylalanine quinone
-
 Ogataea angusta

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.4.3.21 0.09
-
 benzylamine isoform HPAO-1, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta
1.4.3.21 1.2
-
 methylamine isoform HPAO-2, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta
1.4.3.21 30
-
 methylamine isoform HPAO-1, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta
1.4.3.21 81
-
 O2 isoform HPAO-1, using benzylamine as cosubstrate, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta
1.4.3.21 160
-
 O2 isoform HPAO-2, using methylamine as cosubstrate, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta
1.4.3.21 400
-
 O2 isoform HPAO-1, using methylamine as cosubstrate, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta
1.4.3.21 470
-
 O2 isoform HPAO-2, using benzylamine as cosubstrate, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta
1.4.3.21 900
-
 benzylamine isoform HPAO-2, at 25°C, in 100 mM potassium phosphate, pH 7.2 Ogataea angusta