메뉴 건너뛰기




Volumn 18, Issue 7, 2002, Pages 302-308

The diversity and evolution of thioredoxin reductase: New perspectives

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE REDUCTASE; THIOREDOXIN REDUCTASE;

EID: 0036629836     PISSN: 14714922     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1471-4922(02)02293-6     Document Type: Review
Times cited : (103)

References (57)
  • 2
    • 0034050669 scopus 로고    scopus 로고
    • Free radicals, antioxidants, and the immune system
    • Knight J.A. Free radicals, antioxidants, and the immune system. Ann. Clin. Lab. Sci. 30:2000;145-158.
    • (2000) Ann. Clin. Lab. Sci. , vol.30 , pp. 145-158
    • Knight, J.A.1
  • 4
    • 0033781942 scopus 로고    scopus 로고
    • Thioredoxin reductase two modes of catalysis have evolved
    • Williams C.H., et al. Thioredoxin reductase two modes of catalysis have evolved. Eur. J. Biochem. 267:2000;6110-6117.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6110-6117
    • Williams, C.H.1
  • 5
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arner E.S., Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267:2000;6102-6109.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2
  • 6
    • 0033771121 scopus 로고    scopus 로고
    • Thioredoxin-thioredoxin reductase - a system that has come of age
    • Williams C.H. Thioredoxin-thioredoxin reductase - a system that has come of age. Eur. J. Biochem. 267:2000;6101.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6101
    • Williams, C.H.1
  • 7
    • 0033215010 scopus 로고    scopus 로고
    • Enzymes of parasite thiol metabolism as drug targets
    • Krauth-Siegel R.L., Coombs G.H. Enzymes of parasite thiol metabolism as drug targets. Parasitol. Today. 15:1999;404-409.
    • (1999) Parasitol. Today , vol.15 , pp. 404-409
    • Krauth-Siegel, R.L.1    Coombs, G.H.2
  • 8
    • 0033775650 scopus 로고    scopus 로고
    • Thioredoxin reductase as a pathophysiological factor and drug target
    • Becker K., et al. Thioredoxin reductase as a pathophysiological factor and drug target. Eur. J. Biochem. 267:2000;6118-6125.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6118-6125
    • Becker, K.1
  • 9
    • 0033388744 scopus 로고    scopus 로고
    • News and views on thioredoxin reductases
    • Gromer S., et al. News and views on thioredoxin reductases. Redox Rep. 4:1999;221-228.
    • (1999) Redox Rep. , vol.4 , pp. 221-228
    • Gromer, S.1
  • 10
    • 0032898734 scopus 로고    scopus 로고
    • Cloning, sequencing and functional expression of a novel human thioredoxin reductase
    • Gasdaska P.Y., et al. Cloning, sequencing and functional expression of a novel human thioredoxin reductase. FEBS Lett. 442:1999;105-111.
    • (1999) FEBS Lett. , vol.442 , pp. 105-111
    • Gasdaska, P.Y.1
  • 11
    • 0002597781 scopus 로고    scopus 로고
    • Selenocysteine-containing thioredoxin reductase in C. elegans
    • Gladyshev V.N., et al. Selenocysteine-containing thioredoxin reductase in C. elegans. Biochem. Biophys. Res. Commun. 259:1999;244-249.
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 244-249
    • Gladyshev, V.N.1
  • 12
    • 0035951470 scopus 로고    scopus 로고
    • Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster
    • Kanzok S.M., et al. Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster. Science. 291:2001;643-646.
    • (2001) Science , vol.291 , pp. 643-646
    • Kanzok, S.M.1
  • 13
    • 0030272317 scopus 로고    scopus 로고
    • Recombinant putative glutathione reductase of Plasmodium falciparum exhibits thioredoxin reductase activity
    • Müller S., et al. Recombinant putative glutathione reductase of Plasmodium falciparum exhibits thioredoxin reductase activity. Mol. Biochem. Parasitol. 80:1996;215-219.
    • (1996) Mol. Biochem. Parasitol. , vol.80 , pp. 215-219
    • Müller, S.1
  • 14
    • 0000876731 scopus 로고
    • Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - a family of flavoenzyme transhydrogenases
    • F. Müller. CRC Press
    • Williams C.H. Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - a family of flavoenzyme transhydrogenases. Müller F., Chemistry and Biochemistry of Flavoenzymes. 3:1992;6101 CRC Press.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 6101
    • Williams, C.H.1
  • 15
    • 0033771859 scopus 로고    scopus 로고
    • r thioredoxin reductase
    • r thioredoxin reductase. Eur. J. Biochem. 267:2000;6126-6133.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6126-6133
    • Poole, L.B.1
  • 16
    • 0026422435 scopus 로고
    • Convergent evolution of similar function in two structurally divergent enzymes
    • Kuriyan J., et al. Convergent evolution of similar function in two structurally divergent enzymes. Nature. 352:1991;172-174.
    • (1991) Nature , vol.352 , pp. 172-174
    • Kuriyan, J.1
  • 17
    • 0028220312 scopus 로고
    • Crystal structure of Escherichia coli thioredoxin reductase refined at 2 Å resolution. Implications for a large conformational change during catalysis
    • Waksman G., et al. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 Å resolution. Implications for a large conformational change during catalysis. J. Mol. Biol. 236:1994;800-816.
    • (1994) J. Mol. Biol. , vol.236 , pp. 800-816
    • Waksman, G.1
  • 18
    • 0030887844 scopus 로고    scopus 로고
    • The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli
    • Arscott L.D., et al. The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 94:1997;3621-3626.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 3621-3626
    • Arscott, L.D.1
  • 19
    • 0028914574 scopus 로고
    • Identification of an Entamoeba histolytica gene encoding a protein homologous to prokaryotic disulphide oxidoreductases
    • Bruchhaus I., Tannich E. Identification of an Entamoeba histolytica gene encoding a protein homologous to prokaryotic disulphide oxidoreductases. Mol. Biochem. Parasitol. 70:1995;187-191.
    • (1995) Mol. Biochem. Parasitol. , vol.70 , pp. 187-191
    • Bruchhaus, I.1    Tannich, E.2
  • 20
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul S.F., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:1997;3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 21
    • 0030596199 scopus 로고    scopus 로고
    • A thioredoxin reductase-class of disulphide reductase in the protozoan parasite Giardia duodenalis
    • Brown D.M., et al. A thioredoxin reductase-class of disulphide reductase in the protozoan parasite Giardia duodenalis. Mol. Biochem. Parasitol. 83:1996;211-220.
    • (1996) Mol. Biochem. Parasitol. , vol.83 , pp. 211-220
    • Brown, D.M.1
  • 22
    • 0030091553 scopus 로고    scopus 로고
    • Ancestral relationships of the major eukaryotic lineages
    • Sogin M.L., et al. Ancestral relationships of the major eukaryotic lineages. Microbiologia. 12:1996;17-28.
    • (1996) Microbiologia , vol.12 , pp. 17-28
    • Sogin, M.L.1
  • 24
    • 0032702602 scopus 로고    scopus 로고
    • Reconstructing early events in eukaryotes evolution
    • Roger A.J. Reconstructing early events in eukaryotes evolution. Am. Nat. 154:(Suppl.):1999;S146-S163.
    • (1999) Am. Nat. , vol.154 , Issue.SUPPL.
    • Roger, A.J.1
  • 25
    • 0004553333 scopus 로고    scopus 로고
    • The Giardia genome project database
    • McArthur A.G., et al. The Giardia genome project database. FEMS Microbiol. Lett. 189:2000;271-273.
    • (2000) FEMS Microbiol. Lett. , vol.189 , pp. 271-273
    • McArthur, A.G.1
  • 26
    • 0034653305 scopus 로고    scopus 로고
    • Preliminary profile of the Cryptosporidium parvum genome: An expressed sequence tag and genome survey sequence analysis
    • Strong W.B., Nelson R.G. Preliminary profile of the Cryptosporidium parvum genome: an expressed sequence tag and genome survey sequence analysis. Mol. Biochem. Parasitol. 107:2000;1-32.
    • (2000) Mol. Biochem. Parasitol. , vol.107 , pp. 1-32
    • Strong, W.B.1    Nelson, R.G.2
  • 27
    • 0030997915 scopus 로고    scopus 로고
    • Glutathione reductase turned into trypanothione reductase: Structural analysis of an engineered change in substrate specificity
    • Stoll V.S., et al. Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 36:1997;6437-6447.
    • (1997) Biochemistry , vol.36 , pp. 6437-6447
    • Stoll, V.S.1
  • 28
    • 0025787080 scopus 로고
    • Redox enzyme engineering: Conversion of human glutathione reductase into a trypanothione reductase
    • Bradley M., et al. Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductase. Biochemistry. 30:1991;6124-6127.
    • (1991) Biochemistry , vol.30 , pp. 6124-6127
    • Bradley, M.1
  • 29
    • 0032955828 scopus 로고    scopus 로고
    • Evidence for the co-existence of glutathione reductase and trypanothione reductase in the non-trypanosomatid Euglenozoa: Euglena gracilis Z
    • Montrichard F., et al. Evidence for the co-existence of glutathione reductase and trypanothione reductase in the non-trypanosomatid Euglenozoa: Euglena gracilis Z. FEBS Lett. 442:1999;29-33.
    • (1999) FEBS Lett. , vol.442 , pp. 29-33
    • Montrichard, F.1
  • 30
    • 0033977079 scopus 로고    scopus 로고
    • Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress
    • Krieger S., et al. Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress. Mol. Microbiol. 35:2000;542-552.
    • (2000) Mol. Microbiol. , vol.35 , pp. 542-552
    • Krieger, S.1
  • 31
    • 0038331374 scopus 로고    scopus 로고
    • Identification and functional characterization of thioredoxin from Trypanosoma brucei brucei
    • Reckenfelderbaumer N., et al. Identification and functional characterization of thioredoxin from Trypanosoma brucei brucei. J. Biol. Chem. 275:2000;7547-7552.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7547-7552
    • Reckenfelderbaumer, N.1
  • 32
    • 0034682854 scopus 로고    scopus 로고
    • Twists in catalysis: Alternating conformations of Escherichia coli thioredoxin reductase
    • Lennon B.W., et al. Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Science. 289:2000;1190-1194.
    • (2000) Science , vol.289 , pp. 1190-1194
    • Lennon, B.W.1
  • 33
    • 0032478667 scopus 로고    scopus 로고
    • The role of the C-terminus for catalysis of the large thioredoxin reductase from Plasmodium falciparum
    • Gilberger T.W., et al. The role of the C-terminus for catalysis of the large thioredoxin reductase from Plasmodium falciparum. FEBS Lett. 425:1998;407-410.
    • (1998) FEBS Lett. , vol.425 , pp. 407-410
    • Gilberger, T.W.1
  • 34
    • 0032555276 scopus 로고    scopus 로고
    • Human thioredoxin reductase from HeLa cells: Selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin
    • Gorlatov S.N., Stadtman T.C. Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin. Proc. Natl. Acad. Sci. U. S. A. 95:1998;8520-8525.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 8520-8525
    • Gorlatov, S.N.1    Stadtman, T.C.2
  • 35
    • 0033537705 scopus 로고    scopus 로고
    • Thioredoxin reductase from Plasmodium falciparum: Evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol
    • Wang P.F., et al. Thioredoxin reductase from Plasmodium falciparum: evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol. Biochemistry. 38:1999;3187-3196.
    • (1999) Biochemistry , vol.38 , pp. 3187-3196
    • Wang, P.F.1
  • 36
    • 0032103493 scopus 로고    scopus 로고
    • A hypothesis on the catalytic mechanism of the selenoenzyme thioredoxin reductase
    • Gromer S., et al. A hypothesis on the catalytic mechanism of the selenoenzyme thioredoxin reductase. Biochem. J. 332:1998;591-592.
    • (1998) Biochem. J. , vol.332 , pp. 591-592
    • Gromer, S.1
  • 37
    • 0033831968 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary crystallographic data for rat cytosolic selenocysteine 498 to cysteine mutant thioredoxin reductase
    • Zhong L., et al. Purification, crystallization and preliminary crystallographic data for rat cytosolic selenocysteine 498 to cysteine mutant thioredoxin reductase. Acta Crystallogr. D Biol. Crystallogr. 56:2000;1191-1193.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1191-1193
    • Zhong, L.1
  • 38
    • 0035859927 scopus 로고    scopus 로고
    • Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme
    • Sandalova T., et al. Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme. Proc. Natl. Acad. Sci. U. S. A. 98:2001;9533-9538.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9533-9538
    • Sandalova, T.1
  • 39
    • 0035957325 scopus 로고    scopus 로고
    • Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems
    • Sun Q.-A., et al. Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems. Proc. Natl. Acad. Sci. U. S. A. 98:2001;3673-3678.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 3673-3678
    • Sun, Q.-A.1
  • 40
    • 0029165589 scopus 로고
    • Thioredoxin - a fold for all reasons
    • Martin J.L. Thioredoxin - a fold for all reasons. Structure. 3:1995;245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 41
    • 0035799315 scopus 로고    scopus 로고
    • Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotation during catalysis
    • Wood Z.A., et al. Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotation during catalysis. Biochemistry. 40:2001;3900-3911.
    • (2001) Biochemistry , vol.40 , pp. 3900-3911
    • Wood, Z.A.1
  • 42
    • 0017879559 scopus 로고
    • The structure of the flavoenzyme glutathione reductase
    • Schulz G.E., et al. The structure of the flavoenzyme glutathione reductase. Nature. 273:1978;120-124.
    • (1978) Nature , vol.273 , pp. 120-124
    • Schulz, G.E.1
  • 43
    • 0034731388 scopus 로고    scopus 로고
    • Intersubunit interactions in Plasmodium falciparum thioredoxin reductase
    • Krnajski Z., et al. Intersubunit interactions in Plasmodium falciparum thioredoxin reductase. J. Biol. Chem. 275:2000;40874-40878.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40874-40878
    • Krnajski, Z.1
  • 44
    • 0034538854 scopus 로고    scopus 로고
    • An updated and comprehensive rRNA phylogeny of (crown) eukaryotes based on rate-calibrated evolutionary distances
    • Van de Peer Y., et al. An updated and comprehensive rRNA phylogeny of (crown) eukaryotes based on rate-calibrated evolutionary distances. J. Mol. Evol. 51:2000;565-576.
    • (2000) J. Mol. Evol. , vol.51 , pp. 565-576
    • Van de Peer, Y.1
  • 45
    • 0034602344 scopus 로고    scopus 로고
    • A kingdom-level phylogeny of eukaryotes based on combined protein data
    • Baldauf S.L., et al. A kingdom-level phylogeny of eukaryotes based on combined protein data. Science. 290:2000;972-977.
    • (2000) Science , vol.290 , pp. 972-977
    • Baldauf, S.L.1
  • 46
    • 0029989451 scopus 로고    scopus 로고
    • Evolution of stramenopiles and alveolates as derived by 'substitution rate calibration' of small ribosomal subunit RNA
    • van de Peer Y., et al. Evolution of stramenopiles and alveolates as derived by 'substitution rate calibration' of small ribosomal subunit RNA. J. Mol. Evol. 42:1996;201-210.
    • (1996) J. Mol. Evol. , vol.42 , pp. 201-210
    • Van de Peer, Y.1
  • 47
    • 0031663016 scopus 로고    scopus 로고
    • A revised six-kingdom system of life
    • Cavalier-Smith T. A revised six-kingdom system of life. Biol. Rev. 73:1998;203-266.
    • (1998) Biol. Rev. , vol.73 , pp. 203-266
    • Cavalier-Smith, T.1
  • 48
    • 0034815492 scopus 로고    scopus 로고
    • Chaperonin-60 phylogeny provides further evidence of secondary loss of mitochondria among putative early branching eukaryotes
    • Horner D.S., Embley T.M. Chaperonin-60 phylogeny provides further evidence of secondary loss of mitochondria among putative early branching eukaryotes. Mol. Biol. Evol. 18:2001;1970-1975.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 1970-1975
    • Horner, D.S.1    Embley, T.M.2
  • 49
    • 0032521604 scopus 로고    scopus 로고
    • Recombinant expression and biochemical characterization of an NADPH:flavin oxidoreductase from Entamoeba histolytica
    • Bruchhaus I., et al. Recombinant expression and biochemical characterization of an NADPH:flavin oxidoreductase from Entamoeba histolytica. Biochem. J. 330:1998;1217-1221.
    • (1998) Biochem. J. , vol.330 , pp. 1217-1221
    • Bruchhaus, I.1
  • 50
    • 0029165139 scopus 로고
    • Unique gene organization of thioredoxin and thioredoxin reductase in Mycobacterium leprae
    • Wieles B., et al. Unique gene organization of thioredoxin and thioredoxin reductase in Mycobacterium leprae. Mol. Microbiol. 16:1995;921-929.
    • (1995) Mol. Microbiol. , vol.16 , pp. 921-929
    • Wieles, B.1
  • 51
    • 0021327406 scopus 로고
    • Entamoeba histolytica: A eukaryote without glutathione metabolism
    • Fahey R.C., et al. Entamoeba histolytica: a eukaryote without glutathione metabolism. Science. 224:1984;70-72.
    • (1984) Science , vol.224 , pp. 70-72
    • Fahey, R.C.1
  • 52
    • 0032493647 scopus 로고    scopus 로고
    • Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds
    • Gromer S., et al. Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds. J. Biol. Chem. 273:1998;20096-20101.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20096-20101
    • Gromer, S.1
  • 53
    • 0005204142 scopus 로고    scopus 로고
    • Thioredoxin reductase is essential for the survival of Plasmodium falciparum erythrocytic stages
    • in press
    • Krnajski, K. et al. Thioredoxin reductase is essential for the survival of Plasmodium falciparum erythrocytic stages. J. Biol. Chem. (in press)
    • J. Biol. Chem.
    • Krnajski, K.1
  • 54
    • 0035936820 scopus 로고    scopus 로고
    • Host-like molecules in human malarial parasites
    • Dhar A., et al. Host-like molecules in human malarial parasites. FEBS Lett. 491:2001;166-167.
    • (2001) FEBS Lett. , vol.491 , pp. 166-167
    • Dhar, A.1
  • 55
    • 0035253752 scopus 로고    scopus 로고
    • Transformation of malaria parasites by the spontaneous uptake and expression of DNA from human erythrocytes
    • Deitsch K., et al. Transformation of malaria parasites by the spontaneous uptake and expression of DNA from human erythrocytes. Nucleic Acids Res. 29:2001;850-853.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 850-853
    • Deitsch, K.1
  • 56
    • 0034849408 scopus 로고    scopus 로고
    • MrBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck J.P., Ronquist F. MrBAYES: Bayesian inference of phylogenetic trees. Bioinformatics. 17:2001;754-755.
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 57
    • 0001336205 scopus 로고    scopus 로고
    • Phylogeny inference
    • D.M. et al. Hillis. Sinauer Associates
    • Swofford D.L., et al. Phylogeny inference. Hillis D.M., et al. Molecular Systematics. 1996;407-514 Sinauer Associates.
    • (1996) Molecular Systematics , pp. 407-514
    • Swofford, D.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.