Thioredoxin reductase
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thioredoxin reductase 1
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| Identifiers | |
| Symbol(s) | TXNRD1 |
| Entrez | 7296 |
| OMIM | 601112 |
| RefSeq | NM_003330 |
| UniProt | Q16881 |
| Other data | |
| Locus | Chr. 12 q23-q24.1 |
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thioredoxin reductase 2
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| Identifiers | |
| Symbol(s) | TXNRD2 |
| Entrez | 10587 |
| OMIM | 606448 |
| RefSeq | NM_006440 |
| UniProt | Q9NNW7 |
| Other data | |
| Locus | Chr. 22 q11.21 |
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thioredoxin reductase 3
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| Identifiers | |
| Symbol(s) | TXNRD3 |
| Entrez | 114112 |
| OMIM | 606235 |
| RefSeq | XM_051264 |
| UniProt | Q86VQ6 |
| Other data | |
| Locus | Chr. 3 p13-q13.33 |
Thioredoxin Reductase (TR, TrxR) (EC 1.8.1.9) are the only known enzymes to reduce thioredoxin (Trx). All known kingdom of organisms contain thioredoxin reductase. Two types of thioredoxin reductase evolved independently: prokaryotes, archia and most plants have one type; higher eukaryotes and some plants contain a different one which contains selenocysteine. 3 TRs exist in animals: TR1, TR3 and TGR. Both TR1[1] and TR3[2] are essential proteins for mouse embryogenesis.Since the activity of this enzyme is essential for cell growth and survival, it is a good target for anti-tumor therapy. For example, motexafin gadolinium (MGd) is a new chemotherapeutic agent which selectively targets tumor cells, leading to cell death and apoptosis via inhibition of thioredoxin reductase and ribonucleotide reducatse.
[edit] References
Hashemy, S. I., Ungerstedt, J. S., Zahedi Avval, F., and Holmgren, A. (2006). Motexafin gadolinium, a tumor-selective drug targeting thioredoxin reductase and ribonucleotide reductase. J Biol Chem 281, 10691-10697.
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