Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.3.3 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
Search for more literature for 1.4.3.3

General Stability

General Stability Organism
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

Organism UniProt Comment Textmining
Trigonopsis variabilis
-
-
-

Oxidation Stability

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

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