Literature summary extracted from

Van den Berg, P.A.W.; Mulrooney, S.B.; Gobets, B.; van Stokkum, I.H.M.; van Hoek, A.; Williams, C.H., Jr.; Visser, A.J.W.G.
Exploring the conformational equilibrium of E. coli thioredoxin reductase: characterization of two catalytically important states by ultrafast flavin fluorescence spectroscopy (2001), Protein Sci., 10, 2037-2049.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.8.1.9	C138S	-	Escherichia coli

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.8.1.9	phenyl mercuric acetate	stabilizes enzyme in one of two possible conformations	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.8.1.9	Escherichia coli	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
1.8.1.9	thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+	2 conformations possible, termed FR and FO conformation, which differ in their fluorescence spectroscopic behaviour, their accessibility for inhibitors and in the efficiency of electron transfer to FAD, involving position 138 in the wild-type and the mutant C138S	Escherichia coli	a
1.8.1.9	thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+	electron transfer in the enzyme complex of apoenzyme, FAD and thioredoxin with NADPH	Escherichia coli	a

Synonyms

EC Number	Synonyms	Comment	Organism
1.8.1.9	TrxR	-	Escherichia coli

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.8.1.9	FAD	-	Escherichia coli
1.8.1.9	NADPH	-	Escherichia coli

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Release 2023.1 (January 2023)