Genomes and Genes
Gene Symbol: trxB
Description: thioredoxin reductase, FAD/NAD(P)-binding
Alias: ECK0879, JW0871
Species: Escherichia coli str. K-12 substr. MG1655
- Sardesai A, Gowrishankar J. trans-acting mutations in loci other than kdpDE that affect kdp operon regulation in Escherichia coli: effects of cytoplasmic thiol oxidation status and nucleoid protein H-NS on kdp expression. J Bacteriol. 2001;183:86-93 pubmed..One dke mutation was shown to be in hns, encoding the nucleoid protein H-NS. Another dke mutation was mapped to trxB (encoding thioredoxin reductase), and an equivalent reduction in kdp expression was demonstrated also for trxA ..
- Pan J, Bardwell J. The origami of thioredoxin-like folds. Protein Sci. 2006;15:2217-27 pubmed
- Argyrou A, Blanchard J. Flavoprotein disulfide reductases: advances in chemistry and function. Prog Nucleic Acid Res Mol Biol. 2004;78:89-142 pubmed..Selection of the particular nonflavin redox center and utilization of a second, or even a third, nonflavin redox center in some cases presumably represents the most efficient strategy for reduction of the individual substrate. ..
- Haller B, Fuchs J. Mapping of trxB, a mutation responsible for reduced thioredoxin reductase activity. J Bacteriol. 1984;159:1060-2 pubmedThe mutation (trxB) responsible for reduced thioredoxin reductase activity has been mapped on the Escherichia coli K-12 chromosome clockwise from aroA between 20 and 21 min. The gene order in this region of the E...
- Amegbey G, Monzavi H, Habibi Nazhad B, Bhattacharyya S, Wishart D. Structural and functional characterization of a thioredoxin-like protein (Mt0807) from Methanobacterium thermoautotrophicum. Biochemistry. 2003;42:8001-10 pubmed..thermoautotrophicum, while Mt0895 plays a minor or supportive role. We also suggest that these two molecules (Mt0807 and Mt0895) may represent a group of ancient proteins that were ancestral to both thioredoxins and glutaredoxins. ..
- Fernandes A, Fladvad M, Berndt C, Andrésen C, Lillig C, Neubauer P, et al. A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase. J Biol Chem. 2005;280:24544-52 pubmed..Grx4 was highly elevated upon iron depletion, suggesting an iron-related function for the protein. ..
- Pigiet V, Conley R. Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography. J Biol Chem. 1977;252:6367-72 pubmed..Both reductases exhibit an absorption band at approximately 320 nm which appears due to a residual amount of tightly bound NADP. Presence of this absorption band has no apparent effect on the specific activity of either enzyme. ..
- Knapp K, Swartz J. Cell-free production of active E. coli thioredoxin reductase and glutathione reductase. FEBS Lett. 2004;559:66-70 pubmed..The specific activity for both TR and GR decreased without FAD supplementation. This research demonstrates that CFPS can be used to produce enzymes that are multimeric and require a cofactor. ..
- Ravi D, Das K. Redox-cycling of anthracyclines by thioredoxin system: increased superoxide generation and DNA damage. Cancer Chemother Pharmacol. 2004;54:449-58 pubmed..coli Trx followed by doxorubicin treatment, increased levels of ROS generation were observed. Taken together, these results show a novel property of the Trx system in bioreductive activation of anthracyclines. ..
- Meyer Y, Buchanan B, Vignols F, Reichheld J. Thioredoxins and glutaredoxins: unifying elements in redox biology. Annu Rev Genet. 2009;43:335-67 pubmed publisher..The new information will be important not only to our understanding of the role of Trx and Grx in fundamental cell processes but also to future societal benefits as the proteins find new applications in a range of fields. ..
- Bessette P, Aslund F, Beckwith J, Georgiou G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc Natl Acad Sci U S A. 1999;96:13703-8 pubmed..However, mutants in which the reduction of both thioredoxins and glutathione is impaired (trxB gor mutants) accumulate oxidized, enzymatically active alkaline phosphatase in the cytoplasm...
- Fredriksson A, Nystrom T. Conditional and replicative senescence in Escherichia coli. Curr Opin Microbiol. 2006;9:612-8 pubmed..Thus, bacterial physiology might entail both conditional and mandatory aging processes. ..
- Kuriyan J, Wong L, Russel M, Model P. Crystallization and preliminary x-ray characterization of thioredoxin reductase from Escherichia coli. J Biol Chem. 1989;264:12752-3 pubmed..The space group is P6(3)22 (a = b = 123.8 A, c = 81.6 A), with one monomer of the enzyme (34.5 kDa) in the crystallographic asymmetric unit. The crystals are well ordered and diffract to beyond 2 A resolution. ..
- Nocek B, Jang S, Jeong M, Clark D, Ensign S, Peters J. Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. Biochemistry. 2002;41:12907-13 pubmed..The encapsulation of the substrate in this manner is reminiscent of the conformational changes observed in the well-characterized CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxidase (Rubisco). ..
- Saing K, Orii H, Tanaka Y, Yanagisawa K, Miura A, Ikeda H. Formation of deletion in Escherichia coli between direct repeats located in the long inverted repeats of a cellular slime mold plasmid: participation of DNA gyrase. Mol Gen Genet. 1988;214:1-5 pubmed..These sequences consist of local short inverted repeats, where cutting and rejoining occur at one of the two regions. ..
- Russel M, Model P. Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases. J Biol Chem. 1988;263:9015-9 pubmed
- Reynolds C, Poole L. Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity. Biochemistry. 2000;39:8859-69 pubmed..These studies indicate that the C-terminal part of AhpF and bacterial TrR have very similar mechanistic properties. These findings also confirm that the N-terminal domain of AhpF plays a direct role in AhpC reduction. ..
- Lennon B, Williams C, Ludwig M. Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Science. 2000;289:1190-4 pubmed..Comparison of these structures demonstrates that switching between the two conformations involves a "ball-and-socket" motion in which the pyridine nucleotide-binding domain rotates by 67 degrees...
- Williams C, Arscott L, Muller S, Lennon B, Ludwig M, Wang P, et al. Thioredoxin reductase two modes of catalysis have evolved. Eur J Biochem. 2000;267:6110-7 pubmed..P. falciparum is the major causative agent of malaria and it is hoped that the chemical difference between the two high Mr forms may be exploited for drug design. ..
- Lennon B, Williams C. Enzyme-monitored turnover of Escherichia coli thioredoxin reductase: insights for catalysis. Biochemistry. 1996;35:4704-12 pubmed..These results clarify the mechanism of thioredoxin reductase in relation to the known structure the enzyme, and provide support for earlier work in which we proposed that this enzyme utilizes a ternary complex mechanism in catalysis. ..
- Lee J, Kim M, Cho J, Kim S. Enhanced expression of tandem multimers of the antimicrobial peptide buforin II in Escherichia coli by the DEAD-box protein and trxB mutant. Appl Microbiol Biotechnol. 2002;58:790-6 pubmed..peptide, buforin II, fused to an anionic peptide, we studied the effect of the DEAD-box protein and the trxB mutant on the expression of tandem multimers...
- Cline D, Redding S, Brohawn S, Psathas J, Schneider J, Thorpe C. New water-soluble phosphines as reductants of peptide and protein disulfide bonds: reactivity and membrane permeability. Biochemistry. 2004;43:15195-203 pubmed..In sum, these data suggest that there is considerable scope for the synthesis of phosphine analogues tailored for specific applications in biological systems...
- Waksman G, Krishna T, Williams C, Kuriyan J. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. J Mol Biol. 1994;236:800-16 pubmed..This would alternately place the nicotinamide ring and the disulfide bond near the flavin ring, and expose the cysteine residues for reaction with thioredoxin in the hypothetical conformation.(ABSTRACT TRUNCATED AT 400 WORDS) ..
- Mössner E, Huber Wunderlich M, Rietsch A, Beckwith J, Glockshuber R, Aslund F. Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli. J Biol Chem. 1999;274:25254-9 pubmed
- Faulkner M, Veeravalli K, Gon S, Georgiou G, Beckwith J. Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways. Proc Natl Acad Sci U S A. 2008;105:6735-40 pubmed publisher..Double mutants lacking thioredoxin reductase (trxB) and glutathione reductase (gor) or glutathione biosynthesis (gshA) cannot grow...
- Williams C. Mechanism and structure of thioredoxin reductase from Escherichia coli. FASEB J. 1995;9:1267-76 pubmed..Reverse rotation allows reduction of the redox active disulfide by the reduced flavin. This requires that the enzyme pass through a ternary complex; the kinetic evidence for such a complex is discussed. ..
- van den Berg P, Mulrooney S, Gobets B, Van Stokkum I, van Hoek A, Williams C, et al. Exploring the conformational equilibrium of E. coli thioredoxin reductase: characterization of two catalytically important states by ultrafast flavin fluorescence spectroscopy. Protein Sci. 2001;10:2037-49 pubmed..Raising the temperature from 277K-323K resulted in a moderate shift to the FR conformation for TrxR C138S. High concentrations of the cosolvent glycerol triggered the domain rotation from the FO to the FR conformation. ..
- Proba K, Ge L, Pluckthun A. Functional antibody single-chain fragments from the cytoplasm of Escherichia coli: influence of thioredoxin reductase (TrxB). Gene. 1995;159:203-7 pubmed..coli in the absence of thioredoxin reductase (TrxB) activity. The amount of soluble protein remained largely unchanged by this null mutation...
- Negri A, Rodriguez Larrea D, Marco E, Jimenez Ruiz A, Sanchez Ruiz J, Gago F. Protein-protein interactions at an enzyme-substrate interface: characterization of transient reaction intermediates throughout a full catalytic cycle of Escherichia coli thioredoxin reductase. Proteins. 2010;78:36-51 pubmed publisher..coli TrxR appears as a beautifully engineered molecular machine that is capable of synchronizing cofactor capture and ejection with substrate binding and redox activity through an interdomain twisting motion. ..
- Xiong S, Wang Y, Ren X, Li B, Zhang M, Luo Y, et al. Solubility of disulfide-bonded proteins in the cytoplasm of Escherichia coli and its "oxidizing" mutant. World J Gastroenterol. 2005;11:1077-82 pubmed..Modification of the redox environment of E. coli cytoplasm can significantly improve the folding of recombinant disulfide-bonded proteins produced in it. ..
- Kuriyan J, Krishna T, Wong L, Guenther B, Pahler A, Williams C, et al. Convergent evolution of similar function in two structurally divergent enzymes. Nature. 1991;352:172-4 pubmed..This suggests that these enzymes diverged from an ancestral nucleotide-binding protein and acquired their disulphide reductase activities independently. ..
- Poole L, Reynolds C, Wood Z, Karplus P, Ellis H, Li Calzi M. AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase. Eur J Biochem. 2000;267:6126-33 pubmed
- Prongay A, Engelke D, Williams C. Characterization of two active site mutations of thioredoxin reductase from Escherichia coli. J Biol Chem. 1989;264:2656-64 pubmed..forming this disulfide have been individually changed to serines by site-directed mutageneses of the cloned trxB gene of Escherichia coli...
- Ueshima R, Fujita N, Ishihama A. Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit. Biochem Biophys Res Commun. 1992;184:634-9 pubmed..2 peptide indicated that the anti-sigma peptide serum contained at least three different species of antibodies. All the four SCRPs analyzed here reacted with an antibody against a C-terminus-proximal epitope. ..
- Veine D, Mulrooney S, Wang P, Williams C. Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin. Protein Sci. 1998;7:1441-50 pubmed..These results suggest that Cys138 may be the thiol initiating dithiol-disulfide interchange between thioredoxin reductase and thioredoxin...
- Toledano M, Kumar C, Le Moan N, Spector D, Tacnet F. The system biology of thiol redox system in Escherichia coli and yeast: differential functions in oxidative stress, iron metabolism and DNA synthesis. FEBS Lett. 2007;581:3598-607 pubmed..We show that although prokaryotic and eukaryotic systems have a similar architecture, they profoundly differ in their overall cellular functions. ..
- Ding H, Harrison K, Lu J. Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. J Biol Chem. 2005;280:30432-7 pubmed..The results provide additional evidence for the hypothesis that IscA is capable of recruiting intracellular "free" iron and delivering the iron for the iron-sulfur cluster assembly in IscU. ..
- Kern R, Malki A, Holmgren A, Richarme G. Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase. Biochem J. 2003;371:965-72 pubmed..These results suggest that the thioredoxin system, in addition to its protein disulphide isomerase activity possesses chaperone-like properties, and that its thioredoxin reductase component plays a major role in this function. ..
- Saejung W, Puttikhunt C, Prommool T, Sojikul P, Tanaka R, Fujiyama K, et al. Enhancement of recombinant soluble dengue virus 2 envelope domain III protein production in Escherichia coli trxB and gor double mutant. J Biosci Bioeng. 2006;102:333-9 pubmed..The enhanced production of the soluble protein could be attributed to the thioredoxin reductase (trxB) and glutathione reductase (gor) double mutations in the Origami genome...
- Vlamis Gardikas A. The multiple functions of the thiol-based electron flow pathways of Escherichia coli: Eternal concepts revisited. Biochim Biophys Acta. 2008;1780:1170-200 pubmed publisher..The emerging possibility is the development of novel antibiotics. ..
- Mulrooney S, Williams C. Potential active-site base of thioredoxin reductase from Escherichia coli: examination of histidine245 and aspartate139 by site-directed mutagenesis. Biochemistry. 1994;33:3148-54 pubmed..23 s-1-about 1% that of wild-type enzyme. We suggest that Asp139 is the active-site acid catalyst which functions to protonate the thiolate anion of reduced thioredoxin.(ABSTRACT TRUNCATED AT 250 WORDS) ..
- Moore E, Reichard P, Thelander L. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES.V. PURIFICATION AND PROPERTIES OF THIOREDOXIN REDUCTASE FROM ESCHERICHIA COLI B. J Biol Chem. 1964;239:3445-52 pubmed
- Sigdel T, Cilliers R, Gursahaney P, Thompson P, Easton J, Crowder M. Probing the adaptive response of Escherichia coli to extracellular Zn(II). Biometals. 2006;19:461-71 pubmed..coli proteins, and the results are discussed in light of recent genomic profiling studies on the adaptive response of E. coli cells to stress by Zn(II) excess. ..
- Takahata M, Tamura T, Abe K, Mihara H, Kurokawa S, Yamamoto Y, et al. Selenite assimilation into formate dehydrogenase H depends on thioredoxin reductase in Escherichia coli. J Biochem. 2008;143:467-73 pubmed publisher..The novel conditions allowed us to study the effects of disrupting genes like trxB (thioredoxin reductase) or gor (glutathione reductase) on the production of FDH H activity and also reductive ..
- Poole R, Hatch L, Cleeter M, Gibson F, Cox G, Wu G. Cytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter. Mol Microbiol. 1993;10:421-30 pubmed..The complete nucleotide sequence of the ClaI-HindIII fragment reveals three open reading frames, one being trxB (19.3 min on the E...