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Literature summary for 1.8.1.9 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.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
C138S
-
Escherichia coli

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ electron transfer in the enzyme complex of apoenzyme, FAD and thioredoxin with NADPH Escherichia coli

Synonyms

Synonyms Comment Organism
TrxR
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD
-
Escherichia coli
NADPH
-
Escherichia coli