Difference between revisions of "Thioredoxin reductase"
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Communicated by [[Iglesias-Gonzalez J]] 2019-05-10. | |||
The thioredoxin reductases (TrxRs) is the only known family of enzymes able to reduce thioredoxin in mammals, catalysing the NADPH-dependent reduction of the redox protein thioredoxin (Trx). Three different isoforms have been described for the mammalian TrxRs: TrxR1 (cytosolic), TrxR2 (mitochondrial) and TrxR3 (testis-specific). All of them contains an NADPH and FAD-binding domain, being the net reaction the same but differing in the enzymatic mechanism and their regulation. TrxRs are important for maintaining many aspects of the cell function and can also play a role against oxidant injury, cell growth and transformation, and the recycling of ascorbate from its oxidized form. Moreover, the activity of the enzyme is highly dependant on the availability of selenium. Since TrxRs are able to reduce the number of substrates other than Trx, it is likely that additional biological effects will be discovered for TrxR. Furthermore, inhibiting TrxR with drugs, like [[auranofin]], may lead to new treatments for human diseases such as cancer, AIDS and autoimmune diseases. | |||
Revision as of 15:59, 10 May 2019
- high-resolution terminology - matching measurements at high-resolution
Thioredoxin reductase
Description
Thioredoxin reductase (TrxR).
Abbreviation: AF
MitoPedia topics: Enzyme
Communicated by Iglesias-Gonzalez J 2019-05-10.
The thioredoxin reductases (TrxRs) is the only known family of enzymes able to reduce thioredoxin in mammals, catalysing the NADPH-dependent reduction of the redox protein thioredoxin (Trx). Three different isoforms have been described for the mammalian TrxRs: TrxR1 (cytosolic), TrxR2 (mitochondrial) and TrxR3 (testis-specific). All of them contains an NADPH and FAD-binding domain, being the net reaction the same but differing in the enzymatic mechanism and their regulation. TrxRs are important for maintaining many aspects of the cell function and can also play a role against oxidant injury, cell growth and transformation, and the recycling of ascorbate from its oxidized form. Moreover, the activity of the enzyme is highly dependant on the availability of selenium. Since TrxRs are able to reduce the number of substrates other than Trx, it is likely that additional biological effects will be discovered for TrxR. Furthermore, inhibiting TrxR with drugs, like auranofin, may lead to new treatments for human diseases such as cancer, AIDS and autoimmune diseases.
