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Literature summary 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

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

Protein Variants

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

Organism

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

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.9 thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ catalytic mechanism 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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH i.e. DTNB Escherichia coli 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH coupled assay Escherichia coli 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 thioredoxin + NADP+ coupled assay with DTNB Escherichia coli thioredoxin disulfide + NADPH
-
 ?

Cofactor

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