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Literature summary extracted from

  • Park, U.H.; Han, H.S.; Um, E.; An, X.H.; Kim, E.J.; Um, S.J.
    Redox regulation of transcriptional activity of retinoic acid receptor by thioredoxin glutathione reductase (TGR) (2009), Biochem. Biophys. Res. Commun., 390, 241-246.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.7 expressed in NIH-3T3, TM-3, MSC-1, and TM-4 cells Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.7 Mus musculus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.7 GSSG + NADPH + H+
-
Mus musculus GSH + NADP+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.8.1.7 TGR
-
Mus musculus
1.8.1.7 thioredoxin glutathione reductase
-
Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.7 FAD
-
Mus musculus
1.8.1.7 NADPH
-
Mus musculus

General Information

EC Number General Information Comment Organism
1.8.1.7 physiological function thioredoxin glutathione reductase binding to retinoic acid receptor is required for the retinoic acid-dependent retinoic acid receptor association with chromatin, retinoic acid receptor activity damaged by oxidative stress is restored by thioredoxin glutathione reductase Mus musculus