Protein Variants | Comment | Organism |
---|---|---|
C106C108-(SO2H) | oxidatively modified enzyme shows 75% loss of activity | Trigonopsis variabilis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
80000 | - |
gel filtration | Trigonopsis variabilis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Trigonopsis variabilis | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
TvDAO | - |
Trigonopsis variabilis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
thermal inactivation of D-amino acid oxidase from Trigonopsis variabilis occurs via three parallel paths of irreversible denaturation | Trigonopsis variabilis |
50 | - |
half-life time of native enzyme is 1.69 h, half-life time of oxidatively modified enzyme C106C108-(SO2H) is 0.85 h. Thermal inactivation of D-amino acid oxidase from Trigonopsis variabilis occurs via three parallel paths of irreversible denaturation. One main path leading to inactivation is FAD release, a process whose net rate is 25-fold lower in the oxidized form of TvDAO. Cofactor dissociation is kinetically coupled to aggregation and can be blocked completely by the addition of free FAD. Aggregation is markedly attenuated in the less stable Cys108-SO2H-containing enzyme. A third, however, slow process is the conversion of the native enzyme into the oxidized form | Trigonopsis variabilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Trigonopsis variabilis |