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

BRENDA support

Literature summary for 1.4.3.3 extracted from

  • Slavica, A.; Dib, I.; Nidetzky, B.
    Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences (2005), Appl. Environ. Microbiol., 71, 8061-8068.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information oxidation of Cys108 into cysteine sulfinic acid causes a global conformational response that affects the protein environment of the FAD cofactor. In comparison with the native enzyme, the mutation results in a fourfold-decreased specific activity, reflecting a catalytic efficiency for reduction of dioxygen lowered by about the same factor, and a markedly decreased propensity to aggregate under conditions of thermal denaturation Trigonopsis variabilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
x * 39000, SDS-PAGE Trigonopsis variabilis

Organism

Organism UniProt Comment Textmining
Trigonopsis variabilis Q6R4Q9
-
-
Trigonopsis variabilis Q99042
-
-

Subunits

Subunits Comment Organism
? x * 39000, SDS-PAGE Trigonopsis variabilis

Synonyms

Synonyms Comment Organism
DAAO
-
Trigonopsis variabilis
DAMOX
-
Trigonopsis variabilis
DAO
-
Trigonopsis variabilis
DAO1
-
Trigonopsis variabilis
 LH99
-
Trigonopsis variabilis

Cofactor

Cofactor Comment Organism Structure
FAD
-
Trigonopsis variabilis