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Volumn 16, Issue 2, 2009, Pages 196-200

Trypanothione reductase from Leishmania infantum: Cloning, expression, purification, crystallization and preliminary x-ray data analysis

Author keywords

Drug target; Leishmania infantum; Molecular replacement; Trypanothione reductase; X ray diffraction

Indexed keywords

OXIDOREDUCTASE; RECOMBINANT PROTEIN; TRYPANOTHIONE REDUCTASE;

EID: 63449136128     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609787316306     Document Type: Article
Times cited : (40)

References (25)
  • 1
    • 33750845322 scopus 로고    scopus 로고
    • Alvar, A., Yactayo, S. and Bern C. Leishmaniasis and poverty. (2006) Trends Parasital., 22, 12, 552-557.
    • Alvar, A., Yactayo, S. and Bern C. Leishmaniasis and poverty. (2006) Trends Parasital., 22, 12, 552-557.
  • 2
    • 84934439857 scopus 로고    scopus 로고
    • Singh, G., Jayanarayan, K.G. and Dey, C.S. Arsenite resistance in Leishmania and possible drug targets. (2008) Adv. Exp. Med. Biol., 625, 1-8.
    • Singh, G., Jayanarayan, K.G. and Dey, C.S. Arsenite resistance in Leishmania and possible drug targets. (2008) Adv. Exp. Med. Biol., 625, 1-8.
  • 3
    • 0022002912 scopus 로고    scopus 로고
    • Fairlamb, A.H., Blackburn, P., Ulrich, P., Chait, B.T. and Cerami, A. Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids. (1985) Science, 227, 1485-1487.
    • Fairlamb, A.H., Blackburn, P., Ulrich, P., Chait, B.T. and Cerami, A. Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids. (1985) Science, 227, 1485-1487.
  • 4
    • 13444280474 scopus 로고    scopus 로고
    • Krauth-Siegel, R.L., Bauer, H. and Schirmer, R.H. Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia. (2005) Angew. Chem. Int. Ed., 44, 690-715.
    • Krauth-Siegel, R.L., Bauer, H. and Schirmer, R.H. Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia. (2005) Angew. Chem. Int. Ed., 44, 690-715.
  • 5
    • 33645883558 scopus 로고    scopus 로고
    • Garcia Liñares, G.E., Ravaschino, E.L. and Rodriguez J.B. Progresses in the field of drug design to combat tropical protozoan parasitic diseases. (2006) Curr. Med. Chem., 13, 335-360.
    • Garcia Liñares, G.E., Ravaschino, E.L. and Rodriguez J.B. Progresses in the field of drug design to combat tropical protozoan parasitic diseases. (2006) Curr. Med. Chem., 13, 335-360.
  • 6
    • 0023051830 scopus 로고    scopus 로고
    • Shames, S.L., Fairlamb, A.H., Cerami, A. and Walsh, C.T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. (1986) Biochemistry, 25, 3519-3526.
    • Shames, S.L., Fairlamb, A.H., Cerami, A. and Walsh, C.T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. (1986) Biochemistry, 25, 3519-3526.
  • 7
    • 0023808976 scopus 로고    scopus 로고
    • Shames, S.L., Kimmel, B.E., Peoples, O.P., Agabian, N. and Walsh, C.T. Trypanothione reductase of Trypanosoma congolense: gene isolation, primary sequence determination, and comparison to glutathione reductase. (1988) Biochemistry, 27, 14, 5014-5019.
    • Shames, S.L., Kimmel, B.E., Peoples, O.P., Agabian, N. and Walsh, C.T. Trypanothione reductase of Trypanosoma congolense: gene isolation, primary sequence determination, and comparison to glutathione reductase. (1988) Biochemistry, 27, 14, 5014-5019.
  • 8
    • 0023278434 scopus 로고    scopus 로고
    • Henderson, G.B., Fairlamb, A.H., Ulrich, P. and Cerami, A. Substrate specificity of the flavoprotein trypanothione disulfide reductase from Crithidia fasciculate. (1987) Biochemistry, 26, 3023-3027.
    • Henderson, G.B., Fairlamb, A.H., Ulrich, P. and Cerami, A. Substrate specificity of the flavoprotein trypanothione disulfide reductase from Crithidia fasciculate. (1987) Biochemistry, 26, 3023-3027.
  • 9
    • 0026002958 scopus 로고    scopus 로고
    • Henderson, G.B., Murgolo, N.J., Kuriyan, J., Osapay, K., Kominos, D., Berry, A., Scrutton, N.S., Hinchliffe, N.W., Perham, R.N. and Cerami, A. Engineering the substrate specificity of glutathione reductase toward that of trypanothione reduction. (1991) Proc. Natl. Acad. Sci. USA, 88, 8769-8773.
    • Henderson, G.B., Murgolo, N.J., Kuriyan, J., Osapay, K., Kominos, D., Berry, A., Scrutton, N.S., Hinchliffe, N.W., Perham, R.N. and Cerami, A. Engineering the substrate specificity of glutathione reductase toward that of trypanothione reduction. (1991) Proc. Natl. Acad. Sci. USA, 88, 8769-8773.
  • 10
    • 0027432023 scopus 로고    scopus 로고
    • Waer, A.F., Smith, K., McKie, J.H., Benson, T., Fairlamb, A.H. and Douglas, K.T. The glutamyl binding site of trypanothione reductase from Crithidia fasciculata: enzyme kinetic properties of gamma-glutamyl-modified substrate analogues. (1993) Biochem. Biophys. Acta, 1203, 93-98.
    • Waer, A.F., Smith, K., McKie, J.H., Benson, T., Fairlamb, A.H. and Douglas, K.T. The glutamyl binding site of trypanothione reductase from Crithidia fasciculata: enzyme kinetic properties of gamma-glutamyl-modified substrate analogues. (1993) Biochem. Biophys. Acta, 1203, 93-98.
  • 11
    • 0029360570 scopus 로고    scopus 로고
    • Krauth-Siegel, R.L. and Schoneck, A.R. Flavoprotein structure and mechanism. 5. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design. (1995) FASEB J., 9, 1138.
    • Krauth-Siegel, R.L. and Schoneck, A.R. Flavoprotein structure and mechanism. 5. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design. (1995) FASEB J., 9, 1138.
  • 12
    • 0030926411 scopus 로고    scopus 로고
    • Dumas, C., Ouellette, M., Tovar, J., Cunningham, M.L., Fairlamb, A.H., Tamar, S., Olivier, M. and Papadopoulou, B. Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages. (1997) EMBO J., 16, 2590-2598.
    • Dumas, C., Ouellette, M., Tovar, J., Cunningham, M.L., Fairlamb, A.H., Tamar, S., Olivier, M. and Papadopoulou, B. Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages. (1997) EMBO J., 16, 2590-2598.
  • 13
    • 0031854156 scopus 로고    scopus 로고
    • Tovar, J., Wilkinson, S., Mottram, J.C. and Fairlamb, A.H. Evidence that trypanothione reductase is an essential enzyme in Leishmania by targeted replacement of the tryA gene locus. (1998) Mol. Microbiol, 29, 653-660.
    • Tovar, J., Wilkinson, S., Mottram, J.C. and Fairlamb, A.H. Evidence that trypanothione reductase is an essential enzyme in Leishmania by targeted replacement of the tryA gene locus. (1998) Mol. Microbiol, 29, 653-660.
  • 14
    • 0029017095 scopus 로고    scopus 로고
    • Cunningham, M.L. and Fairlamb A.H. Trypanothione reductase from Leishmania donovani. Purification, characterisation and inhibition by trivalent antimonials. (1995) Eur. J. Biochem., 230, 460-468.
    • Cunningham, M.L. and Fairlamb A.H. Trypanothione reductase from Leishmania donovani. Purification, characterisation and inhibition by trivalent antimonials. (1995) Eur. J. Biochem., 230, 460-468.
  • 15
    • 4544289321 scopus 로고    scopus 로고
    • Wyllie, S., Cunningham, M.L. and Fairlamb, A.H. Dual action of antimonial drugs on thiol redox metabolism in the human pathogen Leishmania donovani. (2004) J. Biol. Chem., 279, 39925-39932.
    • Wyllie, S., Cunningham, M.L. and Fairlamb, A.H. Dual action of antimonial drugs on thiol redox metabolism in the human pathogen Leishmania donovani. (2004) J. Biol. Chem., 279, 39925-39932.
  • 16
    • 0034780949 scopus 로고    scopus 로고
    • Sundar S. Drug resistance in Indian visceral Leishmaniasis. (2001) Trop. Med. Int. Health, 6, 849-854.
    • Sundar S. Drug resistance in Indian visceral Leishmaniasis. (2001) Trop. Med. Int. Health, 6, 849-854.
  • 17
    • 0036319712 scopus 로고    scopus 로고
    • Guerin, P.J., Olliaro, P., Sundar, S., Boelaert, M., Croft, S.L., Desjeux, P., Wasunna, M.K. and Bryceson A.D. Visceral leishmaniasis: current status of control, diagnosis, and treatment, and a proposed research and development agenda. (2002) Lancet Infect. Dis., 2, 494-501.
    • Guerin, P.J., Olliaro, P., Sundar, S., Boelaert, M., Croft, S.L., Desjeux, P., Wasunna, M.K. and Bryceson A.D. Visceral leishmaniasis: current status of control, diagnosis, and treatment, and a proposed research and development agenda. (2002) Lancet Infect. Dis., 2, 494-501.
  • 18
    • 4444244846 scopus 로고    scopus 로고
    • Rijal, S., Chappuis, F., Singh, R., Bovier, P.A., Achrya, A., Karki, B.M., Das, M.L., Desjeux, P., Loutan, L. and Koirala, S. Treatment of visceral leishmaniasis in south-eastern Nepal: decreasing efficacy of sodium stibogluconate and need for a policy to limit further decline. (2003) Trans R. Soc. Trop. Med. Hyg., 97, 350-354.
    • Rijal, S., Chappuis, F., Singh, R., Bovier, P.A., Achrya, A., Karki, B.M., Das, M.L., Desjeux, P., Loutan, L. and Koirala, S. Treatment of visceral leishmaniasis in south-eastern Nepal: decreasing efficacy of sodium stibogluconate and need for a policy to limit further decline. (2003) Trans R. Soc. Trop. Med. Hyg., 97, 350-354.
  • 19
    • 0030773120 scopus 로고    scopus 로고
    • Garforth, J., Yin, H., McKie, J.H., Douglas, K.T. and Fairlamb, A.H. Rational design of selective ligands for trypanothione reductase from Trypanosoma cruzi. Structural effects on the inhibition by dibenzazepines based on imipramine. (1997) J. Enzyme Inhib., 12, 161-173.
    • Garforth, J., Yin, H., McKie, J.H., Douglas, K.T. and Fairlamb, A.H. Rational design of selective ligands for trypanothione reductase from Trypanosoma cruzi. Structural effects on the inhibition by dibenzazepines based on imipramine. (1997) J. Enzyme Inhib., 12, 161-173.
  • 20
    • 3142719178 scopus 로고    scopus 로고
    • Saravanamuthu, A., Vickers, T.J., Bond, C.S., Peterson, M.R., Hunter, W.H. and Fairlamb, A.H. Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: a template for drug design. (2004) J. Biol. Chem., 279, 29493-29500.
    • Saravanamuthu, A., Vickers, T.J., Bond, C.S., Peterson, M.R., Hunter, W.H. and Fairlamb, A.H. Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: a template for drug design. (2004) J. Biol. Chem., 279, 29493-29500.
  • 21
    • 34248577040 scopus 로고    scopus 로고
    • Czechowicz, J.A., Wilhelm, A.K., Spalding, M.D., Larson, A.M., Engel, L.K. and Alberg, D.G. The synthesis and inhibitory activity of dethiotrypanothione and analogues against trypanothione reductase. (2007) J. Org. Chem., 11, 72, 3689-3693.
    • Czechowicz, J.A., Wilhelm, A.K., Spalding, M.D., Larson, A.M., Engel, L.K. and Alberg, D.G. The synthesis and inhibitory activity of dethiotrypanothione and analogues against trypanothione reductase. (2007) J. Org. Chem., 11, 72, 3689-3693.
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Otwinowski, Z. and Minor, W. Processing of X-ray diffraction data collected in oscillation mode. (1997) Methods Enzymol., 276, 307-326.
    • Otwinowski, Z. and Minor, W. Processing of X-ray diffraction data collected in oscillation mode. (1997) Methods Enzymol., 276, 307-326.
  • 23
    • 0014432781 scopus 로고    scopus 로고
    • Matthews, B. W. Solvent content of protein crystals. (1968) J. Mol. Biol., 33, 491-497.
    • Matthews, B. W. Solvent content of protein crystals. (1968) J. Mol. Biol., 33, 491-497.
  • 24
    • 0032078747 scopus 로고    scopus 로고
    • Vagin, A. and Teplyakov, A. A translation-function approach for heavy-atom location in macromolecular crystallography. (1998) Acta Cryst. D, 54, 400-402.
    • Vagin, A. and Teplyakov, A. A translation-function approach for heavy-atom location in macromolecular crystallography. (1998) Acta Cryst. D, 54, 400-402.
  • 25
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography. (1994) Acta Cryst., D50, 760-763.
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography. (1994) Acta Cryst., D50, 760-763.


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