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Literature summary extracted from

  • Lennon, B.W.; Williams, C.H., Jr.
    Enzyme-monitored turnover of Escherichia coli thioredoxin reductase: insights for catalysis (1996), Biochemistry, 35, 4704-4712.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.1.9 cysteine 1 redox-active disulfide per subunit Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.9 35300
-
 2 * 35300 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
-
 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+ oxidation-reduction cycle of thioredoxin Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.9 additional information redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors Escherichia coli ?
-
 ?
1.8.1.9 thioredoxin + NADP+
-
 Escherichia coli thioredoxin disulfide + NADPH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.1.9 dimer 2 * 35300 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.1.9 additional information
-
 additional information
-
 Escherichia coli
1.8.1.9 33
-
 FAD
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.9 FAD 2 FAD per dimer Escherichia coli
1.8.1.9 NADP+
-
 Escherichia coli
1.8.1.9 NADPH
-
 Escherichia coli