Thioredoxin

From Wikipedia, the free encyclopedia

Thioredoxin

PDB rendering based on 1aiu.

Available structures: 1aiu, 1auc, 1cqg, 1cqh, 1ert, 1eru, 1erv, 1erw, 1mdi, 1mdj, 1mdk, 1trs, 1tru, 1trv, 1trw, 2hsh, 2hxk, 2ifq, 2iiy, 3trx, 4trx

Identifiers

Symbol(s)

TXN; DKFZp686B1993; MGC61975; TRX

External IDs

OMIM: 187700 MGI: 98874 HomoloGene: 55732

Gene ontology
Molecular Function:	• protein binding • electron carrier activity • protein disulfide oxidoreductase activity • thiol-disulfide exchange intermediate activity
Biological Process:	• electron transport • transport • cell motility • signal transduction • cell-cell signaling • cell proliferation • cell redox homeostasis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003329 (mRNA)
NP_003320 (protein)

NM_011660 (mRNA)
NP_035790 (protein)

Location

Chr 9: 112.05 - 112.06 Mb

Chr 4: 58.04 - 58.05 Mb

Pubmed search

[1]

[2]

Thioredoxins are proteins that act as antioxidants by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. Thioredoxins are found in nearly all known organisms and are essential for life in mammals.^[1]^[2]

Thioredoxin is a 12-kD oxidoreductase enzyme containing a dithiol-disulfide active site. It is ubiquitous and found in many organisms from plants and bacteria to mammals. Multiple in vitro substrates for thioredoxin have been identified, including ribonuclease, choriogonadotropins, coagulation factors, glucocorticoid receptor, and insulin. Reduction of insulin is classically used as an activity test.[supplied by OMIM]^[3]

Thioredoxins are characterized at the level of their amino acid sequence by the presence of two vicinal cysteines in a CXXC motif. These two cysteines are the key to the ability of thioredoxin to reduce other proteins. Thioredoxin proteins also have a characteristic tertiary structure termed the thioredoxin fold.

The thioredoxins are kept in the reduced state by the flavoenzyme thioredoxin reductase, in a NADPH-dependent reaction.^[4] Thioredoxins act as electron donors to peroxidases and ribonucleotide reductase.^[5] The related glutaredoxins share many of the functions of thioredoxins, but are reduced by glutathione rather than a specific reductase.

1 See also
2 References
3 Further reading
4 External links

[edit] See also

RuBisCO - enzyme activity regulated by thioredoxin

[edit] References

^ Holmgren A (1989). "Thioredoxin and glutaredoxin systems". J Biol Chem 264 (24): 13963–6. PMID 2668278.
^ Nordberg J, Arnér E (2001). "Reactive oxygen species, antioxidants, and the mammalian thioredoxin system". Free Radic Biol Med 31 (11): 1287–312. doi:10.1016/S0891-5849(01)00724-9. PMID 11728801.
^ Entrez Gene: TXN thioredoxin.
^ Mustacich D, Powis G. "Thioredoxin reductase". Biochem J 346 Pt 1: 1–8. PMID 10657232.
^ Arnér E, Holmgren A (2000). "Physiological functions of thioredoxin and thioredoxin reductase". Eur J Biochem 267 (20): 6102–9. doi:10.1046/j.1432-1327.2000.01701.x. PMID 11012661.

[edit] Further reading

Arnér ES, Holmgren A (2000). "Physiological functions of thioredoxin and thioredoxin reductase.". Eur. J. Biochem. 267 (20): 6102–9. doi:10.1046/j.1432-1327.2000.01701.x. PMID 11012661.
Nishinaka Y, Masutani H, Nakamura H, Yodoi J (2002). "Regulatory roles of thioredoxin in oxidative stress-induced cellular responses.". Redox Rep. 6 (5): 289–95. doi:10.1179/135100001101536427. PMID 11778846.
Ago T, Sadoshima J (2007). "Thioredoxin and ventricular remodeling.". J. Mol. Cell. Cardiol. 41 (5): 762–73. doi:10.1016/j.yjmcc.2006.08.006. PMID 17007870.
Tonissen KF, Wells JR (1991). "Isolation and characterization of human thioredoxin-encoding genes.". Gene 102 (2): 221–8. doi:10.1016/0378-1119(91)90081-L. PMID 1874447.
Martin H, Dean M (1991). "Identification of a thioredoxin-related protein associated with plasma membranes.". Biochem. Biophys. Res. Commun. 175 (1): 123–8. doi:10.1016/S0006-291X(05)81209-4. PMID 1998498.
Forman-Kay JD, Clore GM, Wingfield PT, Gronenborn AM (1991). "High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution.". Biochemistry 30 (10): 2685–98. doi:10.1021/bi00224a017. PMID 2001356.
Jacquot JP, de Lamotte F, Fontecave M, et al. (1991). "Human thioredoxin reactivity-structure/function relationship.". Biochem. Biophys. Res. Commun. 173 (3): 1375–81. doi:10.1016/S0006-291X(05)80940-4. PMID 2176490.
Forman-Kay JD, Clore GM, Driscoll PC, et al. (1990). "A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin.". Biochemistry 28 (17): 7088–97. doi:10.1021/bi00443a045. PMID 2684271.
Tagaya Y, Maeda Y, Mitsui A, et al. (1989). "ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction.". EMBO J. 8 (3): 757–64. PMID 2785919.
Wollman EE, d'Auriol L, Rimsky L, et al. (1988). "Cloning and expression of a cDNA for human thioredoxin.". J. Biol. Chem. 263 (30): 15506–12. PMID 3170595.
Heppell-Parton A, Cahn A, Bench A, et al. (1995). "Thioredoxin, a mediator of growth inhibition, maps to 9q31.". Genomics 26 (2): 379–81. doi:10.1016/0888-7543(95)80223-9. PMID 7601465.
Qin J, Clore GM, Kennedy WM, et al. (1995). "Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B.". Structure 3 (3): 289–97. doi:10.1016/S0969-2126(01)00159-9. PMID 7788295.
Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank.". Gene 150 (2): 243–50. PMID 7821789.
Qin J, Clore GM, Gronenborn AM (1994). "The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin.". Structure 2 (6): 503–22. doi:10.1016/S0969-2126(00)00051-4. PMID 7922028.
Gasdaska PY, Oblong JE, Cotgreave IA, Powis G (1994). "The predicted amino acid sequence of human thioredoxin is identical to that of the autocrine growth factor human adult T-cell derived factor (ADF): thioredoxin mRNA is elevated in some human tumors.". Biochim. Biophys. Acta 1218 (3): 292–6. PMID 8049254.
Qin J, Clore GM, Kennedy WP, et al. (1996). "The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal.". Structure 4 (5): 613–20. doi:10.1016/S0969-2126(96)00065-2. PMID 8736558.
Weichsel A, Gasdaska JR, Powis G, Montfort WR (1996). "Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer.". Structure 4 (6): 735–51. doi:10.1016/S0969-2126(96)00079-2. PMID 8805557.
Andersen JF, Sanders DA, Gasdaska JR, et al. (1997). "Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 --> asparagine mutant.". Biochemistry 36 (46): 13979–88. doi:10.1021/bi971004s. PMID 9369469.
Maruyama T, Kitaoka Y, Sachi Y, et al. (1998). "Thioredoxin expression in the human endometrium during the menstrual cycle.". Mol. Hum. Reprod. 3 (11): 989–93. doi:10.1093/molehr/3.11.989. PMID 9433926.
Sahlin L, Stjernholm Y, Holmgren A, et al. (1998). "The expression of thioredoxin mRNA is increased in the human cervix during pregnancy.". Mol. Hum. Reprod. 3 (12): 1113–7. doi:10.1093/molehr/3.12.1113. PMID 9464857.