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Literature summary extracted from

  • Kirkensgaard, K.G.; Haegglund, P.; Finnie, C.; Svensson, B.; Henriksen, A.
    Structure of Hordeum vulgare NADPH-dependent thioredoxin reductase 2. Unwinding the reaction mechanism (2009), Acta Crystallogr. Sect. D, 65, 932-941.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.9 expressed in Escherichia coli Rosetta (DE3) cells Hordeum vulgare

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.1.9 hanging drop vapor diffusion method, using 24% (w/v) PEG 400, 2% Jeffamine M-600, and 0.1 M citrate buffer pH 3.5 Hordeum vulgare

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.9 Hordeum vulgare A9LN30
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.9 HisTrap HP affinity column chromatography, gel filtration Hordeum vulgare

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.9 thioredoxin disulfide + NADPH + H+
-
Hordeum vulgare thioredoxin + NADP+
-
?

Subunits

EC Number Subunits Comment Organism
1.8.1.9 homodimer x-ray crystallography Hordeum vulgare

Synonyms

EC Number Synonyms Comment Organism
1.8.1.9 NADPH-dependent thioredoxin reductase 2
-
Hordeum vulgare
1.8.1.9 NTR2
-
Hordeum vulgare

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.9 FAD contains one FAD molecule per subunit Hordeum vulgare
1.8.1.9 NADPH dependent on Hordeum vulgare