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Literature summary for 1.8.1.9 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
Search for more literature for 1.8.1.9

Activating Compound

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35300
-
 2 * 35300 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ catalytic mechanism Escherichia coli
a
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ oxidation-reduction cycle of thioredoxin Escherichia coli
a

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 35300 Escherichia coli

Turnover Number [1/s]

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

Cofactor

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