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Literature summary for 1.4.3.3 extracted from

  • Kopf, J.; Hormigo, D.; Garcia, J.L.; Acebal, C.; de la Mata, I.; Arroyo, M.
    Inhibition of recombinant d-amino acid oxidase from Trigonopsis variabilis by salts (2011), Enzyme Res., 2011, 158541.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Trigonopsis variabilis

Inhibitors

Inhibitors Comment Organism Structure
KCl about 30% residual activity at 250 mM KCl Trigonopsis variabilis
NaCl direct inhibition by NaCl is due to FAD dissociation Trigonopsis variabilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-amino acid + H2O + O2 Trigonopsis variabilis
-
2-oxocarboxylate + NH3 + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Trigonopsis variabilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Trigonopsis variabilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-alanine + H2O + O2
-
Trigonopsis variabilis pyruvate + NH3 + H2O2
-
?
D-amino acid + H2O + O2
-
Trigonopsis variabilis 2-oxocarboxylate + NH3 + H2O2
-
?

Synonyms

Synonyms Comment Organism
D-amino acid oxidase
-
Trigonopsis variabilis
DAAO
-
Trigonopsis variabilis

Cofactor

Cofactor Comment Organism Structure
FAD
-
Trigonopsis variabilis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
85
-
NaCl in 100 mM potassium phosphate buffer pH 8.0, at 30°C Trigonopsis variabilis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
300
-
in 100 mM potassium phosphate buffer pH 8.0, at 30°C Trigonopsis variabilis NaCl