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Literature summary extracted from

  • Suske, G.; Wagner, W.; Follmann, H.
    NADPH-dependent thioredoxin reductase and a new thioredoxinn from wheat (1979), Z. Naturforsch. C, 34, 214-221.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.1.9 cysteine part of the active site Triticum aestivum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.9 0.003
-
thioredoxin
-
Triticum aestivum
1.8.1.9 0.0032
-
NADPH
-
Triticum aestivum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.9 65000
-
gel filtration Triticum aestivum

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.9 Triticum aestivum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.9 additional information slowly reduces other proteins, e.g. insulin, lipoate and ribonuclease Triticum aestivum ?
-
?
1.8.1.9 thioredoxin + NADP+ coupled assay with DTNB Triticum aestivum thioredoxin disulfide + NADPH
-
?
1.8.1.9 thioredoxin + NADP+
-
Triticum aestivum thioredoxin disulfide + NADPH + H+
-
?
1.8.1.9 thioredoxin + NADP+ i.e. DTNB Triticum aestivum thioredoxin disulfide + NADPH + H+
-
?

Temperature Optimum [°C]

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.8.1.9 70
-
10 min, complete loss of activity Triticum aestivum

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.9 NADPH
-
Triticum aestivum