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Literature summary for 1.4.3.21 extracted from

  • DuBois, J.L.; Klinman, J.P.
    Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha (2006), Biochemistry, 45, 3178-3188.
    View publication on PubMed
Search for more literature for 1.4.3.21

Protein Variants

Protein Variants Comment Organism
Y305A mutation has moderate effects on the kinetics of catalysis (2.7fold and 8fold decrease in kcat using ethylamine and benzylamine as substrates), the same mutation slows cofactor formation by about 45-fold relative to that of the wild-type enzyme. The Y305A mutant forms at least two species: primarily topaquinone at lower pH and a species with a blue-shifted absorbance at high pH Ogataea angusta
Y305F the rate of topaquinone formation is reduced 3fold relative to that of wild-type enzyme, 125fold decrease in kcat using ethylamine as substrate Ogataea angusta

Organism

Organism UniProt Comment Textmining
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 ethanal + NH3 + H2O2
-
 ?
methylamine + H2O + O2
-
 Ogataea angusta methanal + NH3 + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
HPAO
-
 Ogataea angusta

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.16
-
 ethylamine pH 7, 37°C, mutant enzyme Y305F Ogataea angusta
7.5
-
 ethylamine pH 7, 37°C, mutant enzyme Y305A Ogataea angusta
20
-
 ethylamine pH 7, 37°C, wild-type enzyme Ogataea angusta