Any feedback?
Literature summary extracted from
- Insights into the specificity of thioredoxin reductase-thioredoxin interactions. A structural and functional investigation of the yeast thioredoxin system (2010), Biochemistry, 49, 3317-3326.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.8.1.9 | - |
Saccharomyces cerevisiae |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.8.1.9 | D146A | inactive | Saccharomyces cerevisiae |
| 1.8.1.9 | K137A | the mutation does not alter enzyme activity | Saccharomyces cerevisiae |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.1.9 | 0.0006 | - |
thioredoxin 2 | wild type enzyme, pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1.8.1.9 | 0.0009 | - |
thioredoxin 2 | mutant enzyme K137A, pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1.8.1.9 | 0.0011 | - |
thioredoxin 3 | wild type enzyme, pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1.8.1.9 | 0.0013 | - |
thioredoxin 1 | wild type enzyme, pH and temperature not specified in the publication | Saccharomyces cerevisiae |  |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.8.1.9 | cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.8.1.9 | 35000 | - |
2 * 35000, X-ray crystallography | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.9 | additional information | Saccharomyces cerevisiae | the yeast enzyme fails to reduce the human and Escherichia coli thioredoxin | ? | - |
? | |
| 1.8.1.9 | thioredoxin 1 + NADP+ + | Saccharomyces cerevisiae | - |
thioredoxin 1 disulfide + NADPH + H+ | - |
? | |
| 1.8.1.9 | thioredoxin 2 + NADP+ | Saccharomyces cerevisiae | - |
thioredoxin 2 disulfide + NADPH + H+ | - |
? | |
| 1.8.1.9 | thioredoxin 3 + NADP+ | Saccharomyces cerevisiae | - |
thioredoxin 3 disulfide + NADPH + H+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.9 | Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.8.1.9 | - |
Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.9 | additional information | the yeast enzyme fails to reduce the human and Escherichia coli thioredoxin | Saccharomyces cerevisiae | ? | - |
? | |
| 1.8.1.9 | thioredoxin 1 + NADP+ + | - |
Saccharomyces cerevisiae | thioredoxin 1 disulfide + NADPH + H+ | - |
? | |
| 1.8.1.9 | thioredoxin 2 + NADP+ | - |
Saccharomyces cerevisiae | thioredoxin 2 disulfide + NADPH + H+ | - |
? | |
| 1.8.1.9 | thioredoxin 3 + NADP+ | - |
Saccharomyces cerevisiae | thioredoxin 3 disulfide + NADPH + H+ | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.8.1.9 | homodimer | 2 * 35000, X-ray crystallography | Saccharomyces cerevisiae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.1.9 | TrxR1 | - |
Saccharomyces cerevisiae |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.1.9 | 34 | - |
thioredoxin 3 | wild type enzyme, pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1.8.1.9 | 42.9 | - |
thioredoxin 2 | wild type enzyme, pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1.8.1.9 | 43.7 | - |
thioredoxin 1 | wild type enzyme, pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1.8.1.9 | 47.1 | - |
thioredoxin 2 | mutant enzyme K137A, pH and temperature not specified in the publication | Saccharomyces cerevisiae |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.9 | FAD | - |
Saccharomyces cerevisiae | |
| 1.8.1.9 | NADP+ | - |
Saccharomyces cerevisiae | |
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 | 31000 | - |
thioredoxin 3 | wild type enzyme, pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1.8.1.9 | 34000 | - |
thioredoxin 1 | wild type enzyme, pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1.8.1.9 | 52000 | - |
thioredoxin 2 | mutant enzyme K137A, pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1.8.1.9 | 73000 | - |
thioredoxin 2 | wild type enzyme, pH and temperature not specified in the publication | Saccharomyces cerevisiae |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
