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Literature summary for 1.4.3.3 extracted from

  • Dib, I.; Slavica, A.; Riethorst, W.; Nidetzky, B.
    Thermal inactivation of D-amino acid oxidase from Trigonopsis variabilis occurs via three parallel paths of irreversible denaturation (2006), Biotechnol. Bioeng., 94, 645-654.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C106C108-(SO2H) oxidatively modified enzyme shows 75% loss of activity Trigonopsis variabilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
gel filtration Trigonopsis variabilis

Organism

Organism UniProt Comment Textmining
Trigonopsis variabilis
-
-
-

Synonyms

Synonyms Comment Organism
TvDAO
-
Trigonopsis variabilis

Temperature Stability [°C]

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

Cofactor Comment Organism Structure
FAD
-
Trigonopsis variabilis