Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • O'Donnell, M.E.; Williams, C.H.
    Reaction of both active site thiols of reduced thioredoxin reductase with N-ethylmaleimide (1985), Biochemistry, 24, 7617-7621.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.1.9 cysteine part of the active site Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.1.9 N-ethylmaleimide reaction only with the reduced enzyme 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+ inhibition mechanism Escherichia coli

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 requires thioredoxin for reduction of 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+
-
Escherichia coli thioredoxin disulfide + NADPH
-
r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.9 25
-
assay at Escherichia coli

Cofactor

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