126.96.36.199 - Thioredoxin-disulfide reductase
- NADP--thioredoxin reductase.
- NADPH:oxidized thioredoxin oxidoreductase.
- NADPH--thioredoxin reductase.
- Thioredoxin reductase (NADPH).
[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
There are no Cofactors for this Enzyme
Thioredoxin reductase contains FAD and NADPH binding domains that are structurally similar to the corresponding domains of the related enzyme glutathione reductase. The relative orientation of these domains is, however, very different in the two enzymes: when the FAD domains of thioredoxin and glutathione reductases are superimposed, the NADPH domain of one is rotated by 66 degrees with respect to the other. The observed binding mode of NADP+ in thioredoxin reductase is non-productive in that the nicotinamide ring is more than 17 A from the flavin ring system. Thioredoxin reductase belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
The most direct pathway for reducing equivalents in turnover would require a ternary complex in which the flavin is reduced by NADPH while thioredoxin is being reduced by the active site dithiol when the enzyme is in the proposed FR conformation (allows flavin reduction by pyridine nucleotide). Following the reversal of rotation, the nascent active site disulfide could be reduced by the newly reduced flavin.
|AA||Uniprot||Uniprot Resid||PDB||PDB Resid|
There are no kinetic parameters information for this Enzyme
- NAD(P)H-dependent thioredoxin-disulfide reductase TrxR is essential for tellurite and selenite reduction and resistance in Bacillus sp. Y3.
- Glutathione and peroxisome redox homeostasis.
- The multiplicity of Thioredoxin systems meets the specific needs of Clostridia
- Nitric oxide and thioredoxin modulate the activity of caspase 9 in HepG2 cells.
- Identification and characterization of archaeal and bacterial F420 -dependent thioredoxin reductases.
- The impact of light and thioredoxins on the plant thiol-disulfide proteome
- CBSX2 is required for the efficient oxidation of chloroplast redox‐regulated enzymes in darkness
- The effect of thioredoxin and prochymosin coexpression on the refolding of recombinant alpaca chymosin.
- NTRC regulates CP12 to activate Calvin-Benson cycle during cold acclimation.
- Deciphering the Role of Selenoprotein M
- Evolutionarily Conserved Role of Thioredoxin Systems in Determining Longevity.