Thioredoxin reductase

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Identifiers
Symbol TXNRD1
Entrez 7296
HUGO 12437
OMIM 601112
RefSeq NM_003330
UniProt Q16881
Other data
EC number 1.8.1.9
Locus Chr. 12 q23-q24.1
thioredoxin reductase 2
Identifiers
Symbol TXNRD2
Entrez 10587
HUGO 18155
OMIM 606448
RefSeq NM_006440
UniProt Q9NNW7
Other data
EC number 1.8.1.9
Locus Chr. 22 q11.21
thioredoxin reductase 3
Identifiers
Symbol TXNRD3
Entrez 114112
HUGO 20667
OMIM 606235
RefSeq XM_051264
UniProt Q86VQ6
Other data
EC number 1.8.1.9
Locus Chr. 3 p13-q13.33

Thioredoxin Reductase (TR, TrxR) (EC 1.8.1.9) are the only known enzymes to reduce thioredoxin (Trx).[1]

Contents

[edit] Diversity

All known kingdom of organisms contain thioredoxin reductase. Two types of thioredoxin reductase evolved independently:

Three TRs exist in animals: TR1, TR3, and TGR. Both TR1[2] and TR3[3] are essential proteins for mouse embryogenesis.

[edit] Clinical significance

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 that selectively targets tumor cells, leading to cell death and apoptosis via inhibition of thioredoxin reductase and ribonucleotide reductase.[4]

[edit] References

  1. ^ Mustacich D, Powis G. "Thioredoxin reductase". Biochem J 346 Pt 1: 1-8. PMID 10657232. 
  2. ^ Jakupoglu C, Przemeck G, Schneider M et al. (2005). "Cytoplasmic thioredoxin reductase is essential for embryogenesis but dispensable for cardiac development". Mol. Cell. Biol. 25 (5): 1980-8. doi:10.1128/MCB.25.5.1980-1988.2005. PMID 15713651. 
  3. ^ Conrad M, Jakupoglu C, Moreno S et al. (2004). "Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function". Mol. Cell. Biol. 24 (21): 9414-23. doi:10.1128/MCB.24.21.9414-9423.2004. PMID 15485910. 
  4. ^ Hashemy S, Ungerstedt J, Zahedi Avval F, Holmgren A (2006). "Motexafin gadolinium, a tumor-selective drug targeting thioredoxin reductase and ribonucleotide reductase". J. Biol. Chem. 281 (16): 10691-7. doi:10.1074/jbc.M511373200. PMID 16481328. 

[edit] External links