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Literature summary extracted from

  • Lacey, B.M.; Eckenroth, B.E.; Flemer, S.; Hondal, R.J.
    Selenium in thioredoxin reductase: a mechanistic perspective (2008), Biochemistry, 47, 12810-12821.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.9 expressed in Escherichia coli ER2566 cells Drosophila melanogaster
1.8.1.9 expressed in Escherichia coli ER2566 cells Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.9 0.22
-
5,5'-dithiobis(2-nitrobenzoic acid) wild type enzyme, in 50 mM potassium phosphate at pH 7.0 Drosophila melanogaster
1.8.1.9 0.41
-
5,5'-dithiobis(2-nitrobenzoic acid) wild type enzyme, in 50 mM potassium phosphate at pH 7.0 Caenorhabditis elegans
1.8.1.9 0.45
-
5,5'-dithiobis(2-nitrobenzoic acid) wild type enzyme, in 50 mM potassium phosphate at pH 7.0 Mus musculus
1.8.1.9 0.53
-
5,5'-dithiobis(2-nitrobenzoic acid) truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0 Caenorhabditis elegans
1.8.1.9 0.83
-
5,5'-dithiobis(2-nitrobenzoic acid) truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0 Mus musculus
1.8.1.9 4.1
-
5,5'-dithiobis(2-nitrobenzoic acid) truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0 Drosophila melanogaster

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.1.9 cytosol
-
Rattus norvegicus 5829
-
1.8.1.9 mitochondrion
-
Mus musculus 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.1.9 selenium the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin Drosophila melanogaster
1.8.1.9 selenium the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin Mus musculus
1.8.1.9 selenium the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin Rattus norvegicus
1.8.1.9 selenium the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin Caenorhabditis elegans
1.8.1.9 selenium the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin Anopheles gambiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.9 55000
-
12% reducing SDS-PAGE Drosophila melanogaster
1.8.1.9 55000
-
12% reducing SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.9 thioredoxin + NADP+ Drosophila melanogaster
-
thioredoxin disulfide + NADPH + H+
-
?
1.8.1.9 thioredoxin + NADP+ Mus musculus
-
thioredoxin disulfide + NADPH + H+
-
?
1.8.1.9 thioredoxin + NADP+ Rattus norvegicus
-
thioredoxin disulfide + NADPH + H+
-
?
1.8.1.9 thioredoxin + NADP+ Caenorhabditis elegans
-
thioredoxin disulfide + NADPH + H+
-
?
1.8.1.9 thioredoxin + NADP+ Anopheles gambiae
-
thioredoxin disulfide + NADPH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.9 Anopheles gambiae
-
-
-
1.8.1.9 Caenorhabditis elegans
-
-
-
1.8.1.9 Drosophila melanogaster
-
-
-
1.8.1.9 Mus musculus
-
-
-
1.8.1.9 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.9 DEAE column column chromatography, 2',5'-ADP Sepharose 4B column chromatography, phenyl Sepharose column chromatography, and Ni-NTA agarose column chromatography Drosophila melanogaster
1.8.1.9 DEAE column column chromatography, 2',5'-ADP Sepharose 4B column chromatography, phenyl Sepharose column chromatography, and Ni-NTA agarose column chromatography Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
-
Drosophila melanogaster 2-nitro-5-thiobenzoate + NADP+
-
?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
-
Mus musculus 2-nitro-5-thiobenzoate + NADP+
-
?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
-
Rattus norvegicus 2-nitro-5-thiobenzoate + NADP+
-
?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
-
Caenorhabditis elegans 2-nitro-5-thiobenzoate + NADP+
-
?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
-
Anopheles gambiae 2-nitro-5-thiobenzoate + NADP+
-
?
1.8.1.9 thioredoxin + NADP+
-
Drosophila melanogaster thioredoxin disulfide + NADPH + H+
-
?
1.8.1.9 thioredoxin + NADP+
-
Mus musculus thioredoxin disulfide + NADPH + H+
-
?
1.8.1.9 thioredoxin + NADP+
-
Rattus norvegicus thioredoxin disulfide + NADPH + H+
-
?
1.8.1.9 thioredoxin + NADP+
-
Caenorhabditis elegans thioredoxin disulfide + NADPH + H+
-
?
1.8.1.9 thioredoxin + NADP+
-
Anopheles gambiae thioredoxin disulfide + NADPH + H+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.8.1.9 thioredoxin reductase
-
Drosophila melanogaster
1.8.1.9 thioredoxin reductase
-
Mus musculus
1.8.1.9 thioredoxin reductase
-
Rattus norvegicus
1.8.1.9 thioredoxin reductase
-
Caenorhabditis elegans
1.8.1.9 thioredoxin reductase
-
Anopheles gambiae
1.8.1.9 TR2
-
Caenorhabditis elegans
1.8.1.9 TR3
-
Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.1.9 2.23
-
5,5'-dithiobis(2-nitrobenzoic acid) wild type enzyme, in 50 mM potassium phosphate at pH 7.0 Caenorhabditis elegans
1.8.1.9 2.53
-
5,5'-dithiobis(2-nitrobenzoic acid) truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0 Caenorhabditis elegans
1.8.1.9 2.62
-
5,5'-dithiobis(2-nitrobenzoic acid) wild type enzyme, in 50 mM potassium phosphate at pH 7.0 Drosophila melanogaster
1.8.1.9 20.85
-
5,5'-dithiobis(2-nitrobenzoic acid) wild type enzyme, in 50 mM potassium phosphate at pH 7.0 Mus musculus
1.8.1.9 21.6
-
5,5'-dithiobis(2-nitrobenzoic acid) truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0 Drosophila melanogaster
1.8.1.9 48.42
-
5,5'-dithiobis(2-nitrobenzoic acid) truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0 Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.9 6.5
-
the truncated enzyme shows a pH optimum for the reduction of 5,5'-dithiobis(2-nitrobenzoic acid) at pH 6.5 Mus musculus
1.8.1.9 7.5
-
the truncated enzyme shows a pH optimum for the reduction of 5,5'-dithiobis(2-nitrobenzoic acid) at pH 7.5 Drosophila melanogaster
1.8.1.9 8 8.5
-
Drosophila melanogaster

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.9 NADPH
-
Drosophila melanogaster
1.8.1.9 NADPH
-
Mus musculus
1.8.1.9 NADPH
-
Rattus norvegicus
1.8.1.9 NADPH
-
Caenorhabditis elegans
1.8.1.9 NADPH
-
Anopheles gambiae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.8.1.9 0.22
-
5,5'-dithiobis(2-nitrobenzoic acid) wild type enzyme, in 50 mM potassium phosphate at pH 7.0 Drosophila melanogaster
1.8.1.9 4.78
-
5,5'-dithiobis(2-nitrobenzoic acid) truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0 Caenorhabditis elegans
1.8.1.9 5.27
-
5,5'-dithiobis(2-nitrobenzoic acid) truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0 Drosophila melanogaster
1.8.1.9 5.45
-
5,5'-dithiobis(2-nitrobenzoic acid) wild type enzyme, in 50 mM potassium phosphate at pH 7.0 Caenorhabditis elegans
1.8.1.9 45.33
-
5,5'-dithiobis(2-nitrobenzoic acid) wild type enzyme, in 50 mM potassium phosphate at pH 7.0 Mus musculus
1.8.1.9 58.33
-
5,5'-dithiobis(2-nitrobenzoic acid) truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0 Mus musculus