Thioredoxin

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. [cite journal |author=Holmgren A |title=Thioredoxin and glutaredoxin systems |url=http://www.jbc.org/cgi/reprint/264/24/13963.pdf |journal=J Biol Chem |volume=264 |issue=24 |pages=13963–6 |year=1989 |pmid=2668278] [cite journal |author=Nordberg J, Arnér E |title=Reactive oxygen species, antioxidants, and the mammalian thioredoxin system |journal=Free Radic Biol Med |volume=31 |issue=11 |pages=1287–312 |year=2001 |pmid=11728801 |doi=10.1016/S0891-5849(01)00724-9]

PBB_Summary
section_title =
summary_text = 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] [cite web | title = Entrez Gene: TXN thioredoxin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7295| accessdate = ]

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. [cite journal |author=Mustacich D, Powis G |title=Thioredoxin reductase |url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=10657232 |journal=Biochem J |volume=346 Pt 1 |issue= |pages=1–8 |year= |pmid=10657232] Thioredoxins act as electron donors to peroxidases and ribonucleotide reductase. [cite journal |author=Arnér E, Holmgren A |title=Physiological functions of thioredoxin and thioredoxin reductase |journal=Eur J Biochem |volume=267 |issue=20 |pages=6102–9 |year=2000 |pmid=11012661 |doi=10.1046/j.1432-1327.2000.01701.x] The related glutaredoxins share many of the functions of thioredoxins, but are reduced by glutathione rather than a specific reductase.

ee also

*RuBisCO - enzyme activity regulated by thioredoxin

References

Further reading

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

External links

* Pfam database - thioredoxin. http://pfam.wustl.edu/cgi-bin/getdesc?acc=PF00085
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