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Encyclopedia > Thioredoxin

Thioredoxins are small proteins involved in thiol-redox processes. They contain two redox-active cysteine residues in their active sites, usually in a CXXC motif. The thioredoxins are kept in the reduced state by the flavoenzyme thioredoxin reductase, in a NADPH-dependent reaction. Thioredoxins act as electron donors to peroxidases and ribonucleotide reductase.


  Results from FactBites:
 
Function of novel mammalian thioredoxin systems (403 words)
An imbalance occurs between oxidants and antioxidants, in favour of oxidants (oxidative stress) has been directly linked to oxidation of proteins DNA and lipids, which may induce a variety of cellular responses through the generation of secondary metabolic reactive oxygen species.
Thioredoxins (Trx) are a class of small 12-kDa redox proteins known to be present in all eukaryotic and prokaryotic organisms.
This has resulted in the identification of a mitochondrial thioredoxin system (Trx2 and TrxR2), a ubiquitous thioredoxin-like protein of unknown function (Txl), two tissue-specific member of the family in human spermatozoa, Sptrx-1 and Sptrx-2.
Cancer Chemoprotection by Selenium and Thioredoxin (1171 words)
One of the selenoproteins induced by pharmacological concentrations of selenium in cell culture is thioredoxin reductase.
In the absence of thioredoxin reductase or in the presence of oxidative conditions there may not be sufficient reduced thioredoxin to meet all the demands of the cell, and proteins containing oxidation-prone cysteines may accumulate in the inactive disulfide state.
These new results confirm that p53 is dependent on thioredoxin reductase in mammalian cells and justify further investigation of the mechanism and consequences of thioredoxin reductase dependence.
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