| EC |
1.8.1.9 |
| Accepted name: |
thioredoxin-disulfide reductase (NADPH) |
| Reaction: |
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ |
| Glossary: |
The term ‘oxidized thioredoxin’ has been replaced by ‘thioredoxin disulfide’ as the former is ambiguous |
| Other name(s): |
NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase (ambiguous) |
| Systematic name: |
thioredoxin:NADP+ oxidoreductase |
| Comments: |
A flavoprotein (FAD). The enzyme restores the activity of thioredoxin by reducing an internal disulfide bridge. cf. EC 1.8.98.8, thioredoxin-disulfide reductase (factor 420-dependent). |
| Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9074-14-0 |
| References: |
| 1. |
Moore, E.C., Reichard, P. and Thelander, L. Enzymatic synthesis of deoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli B. J. Biol. Chem. 239 (1964) 3445–3452. [PMID: 14245401] |
| 2. |
Speranza, M.L., Ronchi, S. and Minchiotti, L. Purification and characterization of yeast thioredoxin reductase. Biochim. Biophys. Acta 327 (1973) 274–281. [DOI] [PMID: 4149839] |
| 3. |
Arner, E.S. and Holmgren, A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267 (2000) 6102–6109. [DOI] [PMID: 11012661] |
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| [EC 1.8.1.9 created 1972 as EC 1.6.4.5, transferred 2002 to EC 1.8.1.9, modified 2025] |
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