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 | UniProt | Comment | Textmining |
---|---|---|---|
Ogataea angusta | - |
- |
- |
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 | Comment | Organism |
---|---|---|
HPAO | - |
Ogataea angusta |
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 |