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Literature summary for 1.8.1.9 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
Search for more literature for 1.8.1.9

Activating Compound

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Triticum aestivum
-
-
-

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Triticum aestivum