Literature summary for 1.8.1.9 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.

Search for more literature for 1.8.1.9

Protein Variants

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

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	-	-	-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Drosophila melanogaster
NADPH	-	Drosophila melanogaster

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Release 2023.1 (January 2023)