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Literature summary for 1.8.1.9 extracted from

  • Veine, D.M.; Mulrooney, S.B.; Wang, P.F.; Williams, C.H., Jr.
    Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin (1998), Protein Sci., 7, 1441-1450.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
cysteine 2 pairs of cysteine residues, C32, C35 and C135, C138 Escherichia coli

Protein Variants

Protein Variants Comment Organism
C135S fluorescence spectroscopic investigation of the interaction with the flavin group Escherichia coli
C135S exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 138 is remaining Escherichia coli
C135S/C35S fluorescence spectroscopic investigation of the interaction with the flavin group Escherichia coli
C138S fluorescence spectroscopic investigation of the interaction with the flavin group Escherichia coli
C138S exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 135 is remaining, very low activity Escherichia coli
C138S/C35S fluorescence spectroscopic investigation of the interaction with the flavin group Escherichia coli
C32S fluorescence spectroscopic investigation of the interaction with the flavin group Escherichia coli
C32S exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 35 is remaining, low activity Escherichia coli
C35S fluorescence spectroscopic investigation of the interaction with the flavin group Escherichia coli
C35S exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 32 is remaining Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes Escherichia coli

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH i.e. DTNB Escherichia coli 2-nitro-5-thiobenzoate + NADP+
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH coupled assay Escherichia coli 2-nitro-5-thiobenzoate + NADP+
-
?
thioredoxin + NADP+ coupled assay with DTNB Escherichia coli thioredoxin disulfide + NADPH
-
?

Cofactor

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