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Literature summary extracted from

  • Nidetzky, B.
    Stability and stabilization of D-amino acid oxidase from the yeast Trigonopsis variabilis (2007), Biochem. Soc. Trans., 35, 1588-1592.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.4.3.3 covalent modification of DAO using maleimide-activated PEG5000 yields a stable bionconjugate in which three exposed cysteine side chains are derivatized, the PEGylated enzyme shows approximately 3.3fold slowed dissociation of the FAD cofactor at 50°C, and this causes a 2fold thermostabilization of the enzyme activity Trigonopsis variabilis

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.3 Trigonopsis variabilis
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.4.3.3 oxidation of Cys108 into a stable cysteine sulfinic acid causes both decreased activity and stability of the enzyme Trigonopsis variabilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.3 cephalosporin C + H2O + O2
-
 Trigonopsis variabilis 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
 ?
1.4.3.3 D-methionine + H2O + O2
-
 Trigonopsis variabilis 4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.3.3 D-amino acid oxidase
-
 Trigonopsis variabilis
1.4.3.3 DAO
-
 Trigonopsis variabilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.3 FAD dependent, dissociation of FAD is a main contributor to the loss of activity Trigonopsis variabilis