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Literature summary extracted from

  • Huang, H.H.; Arscott, L.D.; Ballou, D.P.; Williams, C.H.
    Function of Glu-469 in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster (2008), Biochemistry, 47, 12769-12776.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.9 E469A the mutant retains 28% of the wild type activity Drosophila melanogaster
1.8.1.9 E469Q the mutant retains 35% of the wild type activity Drosophila melanogaster
1.8.1.9 E470A the mutant retains 70% of the wild type activity Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.9 Drosophila melanogaster
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.9 thioredoxin disulfide + NADPH + H+
-
Drosophila melanogaster thioredoxin + NADP+
-
r

Synonyms

EC Number Synonyms Comment Organism
1.8.1.9 EC 1.6.4.5 formerly Drosophila melanogaster
1.8.1.9 thioredoxin reductase
-
Drosophila melanogaster
1.8.1.9 TrxR
-
Drosophila melanogaster

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.9 FAD
-
Drosophila melanogaster
1.8.1.9 NADPH
-
Drosophila melanogaster