Thioredoxin Reductases

Thioredoxin reductase (TrxR), or thioredoxin disulfide reductase (EC 1.8.1.9), is a component of the thioredoxin system, along with NADPH and thioredoxin, which is critical for maintaining redox function and preventing oxidative stress.

Products
Background
Literature
Gene Data

Inhibitors

Cat No Product Name / Activity
4600 Auranofin
Thioredoxin reductase inhibitor; induces MPT
5921 D9
Potent thioredoxin reductase (TrxR) inhibitor
6189 Myricetin
Irreversible TrxR inhibitor
4996 PMX 464
Putative inhibitor of the Trx-TrxR system; antiproliferative
2954 PX 12
Thioredoxin-1 inhibitor

Thioredoxin reductase (TrxR), or thioredoxin disulfide reductase (EC 1.8.1.9), is a component of the thioredoxin system, along with NADPH and thioredoxin, which is critical for maintaining redox function and preventing oxidative stress.

There are two TrxR variants, low molecular weight TrxR (L-TrxR), a 70-kDa protein present in bacteria, fungi and plants, and high molecular weight TrxR (H-TrxR), a 112-130 kDa protein found in higher eukaryotes. In mammals there are three isoforms of H-TrxR: TrxR1, found in the cytoplasm; TrxR2, found in mitochondria; and TrxR3 (also known as thioredoxin glutathione reductase or TGR), found only in specialized tissues, such as the testis.

The enzyme is a member of the pyridine nucleotide-disulfide oxidoreductase family, which includes glutathione reductase, many of which have the same N-terminal active site motif, CVNVGC. Mammalian TrxR contains a selenocysteine residue in the C-terminal motif, which is conserved across species and is essential for catalytic activity. TrxR is a homodimeric enzyme, which in conjunction with NADPH, functions to reduce the active site disulfide of thioredoxin to a dithiol. It also has a broad range of other substrates, including protein disulfide isomerase (PDI), glutaredoxin2 and lipoic acid. The enzyme has two catalytically important redox sites, one comprising flavin adenine dinucleotide (FAD) and nearby Cys residues, which receives electrons from NADPH, and the other consisting of the C-terminal motif that receives electrons from the other catalytic site and transfers them to Trx.

The thioredoxin system is ubiquitous across species, and in mammals it works in conjunction with the glutathione system to control the cellular redox environment. TrxR is involved in all biochemical pathways in which Trx has a role as a reducing substrate, and as such is of interest in multiple physiological and pathological processes, including apoptosis, cancer, autoimmune diseases, chronic inflammation and neurodegenerative disorders. TrxR and Trx are overexpressed in many cancers, with cancer cell growth being dependent on the Trx system, so TrxR may be a target for cancer therapy. In addition a number of bacteria, including Mycobacterium tuberculosis and Helicobacter pylori are lacking the glutathione antioxidant system making TrxR a potential target for antibacterials.

Literature for Thioredoxin Reductases

Tocris offers the following scientific literature for Thioredoxin Reductases to showcase our products. We invite you to request* or download your copy today!

*Please note that Tocris will only send literature to established scientific business / institute addresses.


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Thioredoxin Reductase Gene Data

Gene Species Gene Symbol Gene Accession No. Protein Accession No.
Thioredoxin Reductase 1 Human TXNRD1 NM_003330 Q16881
Mouse Txnrd1 NM_001042523 Q9JMH6
Rat Txnrd1 NM_031614 O89049
Thioredoxin Reductase 2 Human TXNRD2 NM_006440 Q9NNW7
Mouse Txnrd2 NM_013711 Q9JLT4
Rat Txnrd2 NM_022584 Q9Z0J5
Thioredoxin Reductase 3 Human TXNRD3 XM_051264 Q86VQ6
Mouse Txnrd3 NM_001178058 Q99MD6
Rat Txnrd3 NM_001106609 NP_001100079