Name | thioredoxin |
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Synonyms | ADF; TRX 1; TRX1; ATL derived factor; SASP; Surface associated sulphydryl protein; TRDX; TRX… |
Name | sulfoxide |
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CAS | 5-[2-(octylsulfinyl)propyl]-1,3-benzodioxole |
PubMed | Abstract | RScore(About this table) | |
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18255097 | Ranaivoson FM, Antoine M, Kauffmann B, Boschi-Muller S, Aubry A, Branlant G, Favier F: A structural analysis of the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis. J Mol Biol. 2008 Mar 14;377(1):268-80. Epub 2008 Jan 16. The reductases (Msrs) are thioredoxin-dependent oxidoreductases that catalyse the reduction of the sulfoxide function of the oxidized residues. |
32(0,1,1,2) | Details |
17761174 | Vieira Dos Santos C, Laugier E, Tarrago L, Massot V, Issakidis-Bourguet E, Rouhier N, Rey P: Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial reductases B. FEBS Lett. 2007 Sep 18;581(23):4371-6. Epub 2007 Aug 14. |
3(0,0,0,3) | Details |
20236937 | Tarrago L, Laugier E, Zaffagnini M, Marchand CH, Le Marechal P, Lemaire SD, Rey P: The plant thioredoxin CDSP32 regenerates 1-CYS methionine sulfoxide reductase B activity through the direct reduction of sulfenic acid. J Biol Chem. 2010 Mar 17. |
2(0,0,0,2) | Details |
20306235 | Hawkes WC, Alkan Z: Regulation of Redox Signaling by Selenoproteins. Biol Trace Elem Res. 2010 Mar 20. Thioredoxin reductases (three genes) use to reduce oxidized thioredoxin and its homologs, which regulate a plethora of redox signaling events. |
2(0,0,0,2) | Details |
18990697 | Fomenko DE, Novoselov SV, Natarajan SK, Lee BC, Koc A, Carlson BA, Lee TH, Kim HY, Hatfield DL, Gladyshev VN: MsrB1 (methionine-R-sulfoxide reductase 1) knock-out mice: roles of MsrB1 in redox regulation and identification of a novel selenoprotein form. J Biol Chem. 2009 Feb 27;284(9):5986-93. Epub 2008 Nov 6. residues are particularly susceptible to oxidation, but the resulting mixture of R-sulfoxide (Met-RO) and S-sulfoxide (Met-SO) can be repaired by thioredoxin-dependent enzymes MsrB and MsrA, respectively. |
31(0,1,1,1) | Details |
19733575 | Ranaivoson FM, Neiers F, Kauffmann B, Boschi-Muller S, Branlant G, Favier F: Methionine sulfoxide reductase B displays a high level of flexibility. J Mol Biol. 2009 Nov 20;394(1):83-93. Epub 2009 Sep 4. MsrB are stereospecific to R epimer on the of sulfoxide. For the subclass of MsrB whose recycling process passes through the formation of an intradisulfide bond, the recycling reducer is thioredoxin. |
2(0,0,0,2) | Details |
18452709 | Kim HY, Kim JR: Thioredoxin as a reducing agent for mammalian reductases B lacking resolving Biochem Biophys Res Commun. 2008 Jul 4;371(3):490-4. Epub 2008 Apr 29. |
2(0,0,0,2) | Details |
19958171 | Ugarte N, Petropoulos I, Friguet B: Oxidized Mitochondrial Protein Degradation and Repair in Aging and Oxidative Stress. Antioxid Redox Signal. 2010 Mar 8. Oxidized protein repair systems, thioredoxin/thioredoxin reductase or glutaredoxin/ /glutathione reductase that catalytically reduce disulfide bridges or sulfenic acids, and reductase that reverses back to within proteins, are present in the mitochondrial matrix. |
1(0,0,0,1) | Details |
17500063 | Gand A, Antoine M, Boschi-Muller S, Branlant G: Characterization of the amino acids involved in substrate specificity of methionine sulfoxide reductase A. J Biol Chem. 2007 Jul 13;282(28):20484-91. Epub 2007 May 11. reductases (Msrs) are ubiquitous enzymes that catalyze the thioredoxin-dependent reduction of (MetSO) back to MsrAs are stereo-specific toward the S epimer on the of the sulfoxide, whereas MsrBs are specific toward the R isomer. |
1(0,0,0,1) | Details |
19457862 | Tarrago L, Laugier E, Zaffagnini M, Marchand C, Le Marechal P, Rouhier N, Lemaire SD, Rey P: Regeneration mechanisms of Arabidopsis thaliana glutaredoxins and thioredoxins. J Biol Chem. 2009 Jul 10;284(28):18963-71. Epub 2009 May 20. |
reductases B by 2(0,0,0,2) | Details |
18722338 | Lee TH, Kim HY: An anaerobic bacterial MsrB model reveals catalytic mechanisms, advantages, and disadvantages provided by reduction of -R-sulfoxide. Arch Biochem Biophys. 2008 Oct 15;478(2):175-80. Epub 2008 Aug 9. However, a resolving Cys was required for the thioredoxin (Trx)-dependent recycling process of the Sec-containing form. |
and in 1(0,0,0,1) | Details |
18667555 | Atack JM, Kelly DJ: Contribution of the stereospecific Cj0637 and Cj1112 were overexpressed, purified and shown by a coupled thioredoxin-thioredoxin reductase- assay to catalyse the stereospecific reduction of the S and R diastereoisomers, respectively, of the model compound methyl p-tolyl sulphoxide. |
sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni. Microbiology. 2008 Aug;154(Pt 8):2219-30.1(0,0,0,1) | Details |
18206120 | Rouhier N, Koh CS, Gelhaye E, Corbier C, Favier F, Didierjean C, Jacquot JP: Redox based anti-oxidant systems in plants: biochemical and structural analyses. Biochim Biophys Acta. 2008 Nov;1780(11):1249-60. Epub 2008 Jan 16. We provide in this paper a comparative biochemical and structural analysis of the major thiol oxidoreductases (thioredoxin and glutaredoxin) of photosynthetic organisms in relation with their reductases and with target proteins, especially those involved either in the detoxication of peroxides such as peroxide (thiol-peroxidases) or in the repair of oxidized methionines in proteins reductases). |
1(0,0,0,1) | Details |
19665240 | Wu TM, Hsu YT, Sung MS, Hsu YT, Lee TM: Expression of genes involved in redox homeostasis and antioxidant defense in a marine macroalga Ulva fasciata by excess Redox-related genes, methionine sulfoxide reductase A (UfMsrA), thioredoxin (UfTrx), cyclophilin (UfCyp), and ferritin (UfFer) that were up-regulated by excess Cu [Wu, T.M., Lee, T.M., 2008. |
Aquat Toxicol. 2009 Oct 4;94(4):275-85. Epub 2009 Jul 19.1(0,0,0,1) | Details |
18651754 | Quinternet M, Tsan P, Neiers F, Beaufils C, Boschi-Muller S, Averlant-Petit MC, Branlant G, Cung MT: Solution structure and dynamics of the reduced and oxidized forms of the N-terminal domain of PilB from Neisseria meningitidis. Biochemistry. 2008 Aug 19;47(33):8577-89. Epub 2008 Jul 24. The N-terminal domain, which possesses a CXXC motif, was recently shown to regenerate in vitro the reduced forms of the reductase domains of PilB from their oxidized forms, as does the thioredoxin 1 from E. coli, via a disulfide bond exchange. |
1(0,0,0,1) | Details |
17660280 | Fukushima E, Shinka Y, Fukui T, Atomi H, Imanaka T: function at suboptimal growth temperatures. J Bacteriol. 2007 Oct;189(19):7134-44. Epub 2007 Jul 27. reductase (Msr) catalyzes the thioredoxin-dependent reduction and repair of (MetO). |
reductase from the hyperthermophilic archaeon Thermococcus kodakaraensis, an enzyme designed to 1(0,0,0,1) | Details |
17766244 | Neiers F, Sonkaria S, Olry A, Boschi-Muller S, Branlant G: Characterization of the amino acids from Neisseria meningitidis methionine sulfoxide reductase B involved in the chemical catalysis and substrate specificity of the reductase step. J Biol Chem. 2007 Nov 2;282(44):32397-405. Epub 2007 Aug 31. reductases (Msrs) are antioxidant repair enzymes that catalyze the thioredoxin-dependent reduction of back to The Msr family is composed of two structurally unrelated classes of enzymes named MsrA and MsrB, which display opposite stereoselectivities toward the S and R isomers of the sulfoxide function, respectively. |
1(0,0,0,1) | Details |
18513221 | Morel M, Kohler A, Martin F, Gelhaye E, Rouhier N: Comparison of the thiol-dependent antioxidant systems in the ectomycorrhizal Laccaria bicolor and the saprotrophic Phanerochaete chrysosporium. New Phytol. 2008;180(2):391-407. Epub 2008 May 28. The two reducing systems (thioredoxin (Trx) and /glutaredoxin (Grx)) are of particular importance against oxidative insults, both for detoxification, through the regeneration of thiol-peroxidases, and for developmental, physiological and signalling processes. |
1(0,0,0,1) | Details |
19049972 | Le DT, Lee BC, Marino SM, Zhang Y, Fomenko DE, Kaya A, Hacioglu E, Kwak GH, Koc A, Kim HY, Gladyshev VN: Functional analysis of free methionine-R-sulfoxide reductase from Saccharomyces cerevisiae. J Biol Chem. 2009 Feb 13;284(7):4354-64. Epub 2008 Dec 2. Molecular modeling and residue targeting by thioredoxin pointed to Cys (101) as catalytic and Cys (125) as resolving residues in yeast fRMsr. MsrA and MsrB are the best known Msrs that repair -S-sulfoxide (Met-S-SO) and -R-sulfoxide (Met-R-SO) residues in proteins, respectively. |
1(0,0,0,1) | Details |
17460202 | Koc A, Gladyshev VN: reduction and the aging process. Ann N Y Acad Sci. 2007 Apr;1100:383-6. reductases, MsrA and MsrB, are thioredoxin-dependent oxidoreductases that reduce oxidized forms of sulfoxides, in a stereospecific manner. |
1(0,0,0,1) | Details |
18581249 | Vinokur V, Grinberg L, Berenshtein E, Gross M, Moskovitz J, Reznick AZ, Chevion M, Eliashar R: digestive tract of young and old rats. Biogerontology. 2009 Feb;10(1):43-52. Epub 2008 Jun 26. The levels of cytosolic thioredoxin (Trx), thioredoxin reductase (TrxR), and reductase (Msr), all tended to decline with age. |
-centered redox cycle in organs of the aero-1(0,0,0,1) | Details |
18845767 | Luo S, Levine RL: Most cells contain reductases, which catalyze a thioredoxin-dependent reduction of back to |
in proteins defends against oxidative stress. FASEB J. 2009 Feb;23(2):464-72. Epub 2008 Oct 9.1(0,0,0,1) | Details |
17673175 | Ding D, Sagher D, Laugier E, Rey P, Weissbach H, Zhang XH: Studies on the reducing systems for plant and animal thioredoxin-independent reductases B. Biochem Biophys Res Commun. 2007 Sep 28;361(3):629-33. Epub 2007 Jul 25. |
1(0,0,0,1) | Details |