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Volumn 39, Issue 5, 2009, Pages 559-568

Localisation of Plasmodium falciparum uroporphyrinogen III decarboxylase of the heme-biosynthetic pathway in the apicoplast and characterisation of its catalytic properties

Author keywords

Apicoplast; Catalytic efficiency; Heme; Plasmodium falciparum; Uroporphyrinogen decarboxylase; Weak dimer

Indexed keywords

AMINO ACID; BLOOD; CATALYSIS; COLIFORM BACTERIUM; CRYSTAL STRUCTURE; ENZYME ACTIVITY; HOMINID; HOST-PARASITE INTERACTION; MOLECULAR ANALYSIS; MUTATION; PLASTID; PROTEIN; PROTOZOAN; RECOMBINATION;

EID: 59749094634     PISSN: 00207519     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpara.2008.10.011     Document Type: Article
Times cited : (37)

References (39)
  • 3
    • 0030758361 scopus 로고    scopus 로고
    • Heme biosynthesis by the malarial parasite: import of δ aminolevulinate dehydratase from the host red cell
    • Bonday Z.Q., Taketani S., Gupta P.D., and Padmanaban G. Heme biosynthesis by the malarial parasite: import of δ aminolevulinate dehydratase from the host red cell. J. Biol. Chem. 272 (1997) 21839-21846
    • (1997) J. Biol. Chem. , vol.272 , pp. 21839-21846
    • Bonday, Z.Q.1    Taketani, S.2    Gupta, P.D.3    Padmanaban, G.4
  • 4
    • 0033834719 scopus 로고    scopus 로고
    • Import of host δ-aminolevulinate dehydratase into the malarial parasite: identification of a new drug target
    • Bonday Z.Q., Dhanasekaran S., Rangarajan P.N., and Padmanaban G. Import of host δ-aminolevulinate dehydratase into the malarial parasite: identification of a new drug target. Nat. Med. 6 (2000) 898-903
    • (2000) Nat. Med. , vol.6 , pp. 898-903
    • Bonday, Z.Q.1    Dhanasekaran, S.2    Rangarajan, P.N.3    Padmanaban, G.4
  • 6
    • 0020601362 scopus 로고
    • Purification of uroporphyrinogen decarboxylase from human erythrocytes
    • Elder G.H., Tovey J.A., and Sheppard D.M. Purification of uroporphyrinogen decarboxylase from human erythrocytes. Biochem. J. 215 (1983) 45-55
    • (1983) Biochem. J. , vol.215 , pp. 45-55
    • Elder, G.H.1    Tovey, J.A.2    Sheppard, D.M.3
  • 7
    • 34247601638 scopus 로고    scopus 로고
    • Crystal structure of uroporphyrinogen decarboxylase from Bacillus subtilis
    • Fan J., Liu Q., Hao Q., Teng M., and Niu L. Crystal structure of uroporphyrinogen decarboxylase from Bacillus subtilis. J. Bacteriol. 189 (2007) 3573-3580
    • (2007) J. Bacteriol. , vol.189 , pp. 3573-3580
    • Fan, J.1    Liu, Q.2    Hao, Q.3    Teng, M.4    Niu, L.5
  • 8
    • 0025264250 scopus 로고
    • Purification and properties of uroporphyrinogen decarboxylase from Saccharomyces cerevisiae
    • Felix F., and Brouillet N. Purification and properties of uroporphyrinogen decarboxylase from Saccharomyces cerevisiae. Eur. J. Biochem. 188 (1990) 393-403
    • (1990) Eur. J. Biochem. , vol.188 , pp. 393-403
    • Felix, F.1    Brouillet, N.2
  • 12
    • 0033213013 scopus 로고    scopus 로고
    • The plastid in Plasmodium falciparum asexual blood stages: a three dimensional ultrastructural analysis
    • Hopkins J., Fowler R., Krishna S., Wilson I., Mitchell G., and Bannister L. The plastid in Plasmodium falciparum asexual blood stages: a three dimensional ultrastructural analysis. Protist 150 (1999) 283-295
    • (1999) Protist , vol.150 , pp. 283-295
    • Hopkins, J.1    Fowler, R.2    Krishna, S.3    Wilson, I.4    Mitchell, G.5    Bannister, L.6
  • 13
    • 0027235975 scopus 로고
    • Purification and properties of the uroporphyrinogen decarboxylase from Rhodobacter sphaeroides
    • Jones R.M., and Jordan P.M. Purification and properties of the uroporphyrinogen decarboxylase from Rhodobacter sphaeroides. Biochem. J. 293 (1993) 703-712
    • (1993) Biochem. J. , vol.293 , pp. 703-712
    • Jones, R.M.1    Jordan, P.M.2
  • 14
    • 0020569127 scopus 로고
    • Uroporphyrinogen decarboxylase - Purification, properties and inhibition by polychlorinated biphenyl isomers
    • Kawanishi S., Seki Y., and Sano S. Uroporphyrinogen decarboxylase - Purification, properties and inhibition by polychlorinated biphenyl isomers. J. Biol. Chem. 258 (1983) 4285-4292
    • (1983) J. Biol. Chem. , vol.258 , pp. 4285-4292
    • Kawanishi, S.1    Seki, Y.2    Sano, S.3
  • 15
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocyte stages in culture
    • Lambros C., and Vanderberg J.P. Synchronization of Plasmodium falciparum erythrocyte stages in culture. J. Parasitol. 65 (1979) 418-420
    • (1979) J. Parasitol. , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 16
    • 0020569745 scopus 로고
    • Separation of porphyrin isomers by high-performance liquid chromatography
    • Lim C.K., Rideout J.M., and Wright D.J. Separation of porphyrin isomers by high-performance liquid chromatography. Biochem. J. 211 (1983) 435-438
    • (1983) Biochem. J. , vol.211 , pp. 435-438
    • Lim, C.K.1    Rideout, J.M.2    Wright, D.J.3
  • 17
    • 0035941294 scopus 로고    scopus 로고
    • Crystal structure and substrate binding modeling of the uroporphyrinogen III decarboxylase from Nicotiana tabacum: implications for the catalytic mechanism
    • Martins B.M., Grimm B., Mock H.P., Huber R., and Messerschmidt A. Crystal structure and substrate binding modeling of the uroporphyrinogen III decarboxylase from Nicotiana tabacum: implications for the catalytic mechanism. J. Biol. Chem. 276 (2001) 44108-44116
    • (2001) J. Biol. Chem. , vol.276 , pp. 44108-44116
    • Martins, B.M.1    Grimm, B.2    Mock, H.P.3    Huber, R.4    Messerschmidt, A.5
  • 19
    • 35348914343 scopus 로고    scopus 로고
    • An alternative model for haem biosynthesis in the malarial parasite
    • Padmanaban G., Nagaraj V.A., and Rangarajan P.N. An alternative model for haem biosynthesis in the malarial parasite. Trends Biochem. Sci. 32 (2007) 443-449
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 443-449
    • Padmanaban, G.1    Nagaraj, V.A.2    Rangarajan, P.N.3
  • 20
    • 0031008511 scopus 로고    scopus 로고
    • Characterization and crystallization of human uroporphyrinogen decarboxylase
    • Phillips J.D., Whitby F.G., Kushner J.P., and Hill C.P. Characterization and crystallization of human uroporphyrinogen decarboxylase. Protein Sci. 6 (1997) 1343-1346
    • (1997) Protein Sci. , vol.6 , pp. 1343-1346
    • Phillips, J.D.1    Whitby, F.G.2    Kushner, J.P.3    Hill, C.P.4
  • 22
    • 0030811027 scopus 로고    scopus 로고
    • Purification and properties of uroporphyrinogen decarboxylase from human erythrocytes
    • Roberts A.G., and Elder G.H. Purification and properties of uroporphyrinogen decarboxylase from human erythrocytes. Methods Enzymol. 281 (1997) 349-355
    • (1997) Methods Enzymol. , vol.281 , pp. 349-355
    • Roberts, A.G.1    Elder, G.H.2
  • 23
    • 0036230756 scopus 로고    scopus 로고
    • The genome of Plasmodium falciparum encodes an active δ-aminolevulinate acid dehydratase
    • Sato S., and Wilson R.J. The genome of Plasmodium falciparum encodes an active δ-aminolevulinate acid dehydratase. Curr. Genet. 40 (2002) 391-398
    • (2002) Curr. Genet. , vol.40 , pp. 391-398
    • Sato, S.1    Wilson, R.J.2
  • 24
    • 1942444611 scopus 로고    scopus 로고
    • Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum
    • Sato S., Clough B., Coates L., and Wilson R.J. Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum. Protist 155 (2004) 117-125
    • (2004) Protist , vol.155 , pp. 117-125
    • Sato, S.1    Clough, B.2    Coates, L.3    Wilson, R.J.4
  • 25
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede J., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31 (2003) 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, J.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 26
    • 28244493956 scopus 로고    scopus 로고
    • Stage-specific cytosolic protein kinase C-like activity in human malarial parasite Plasmodium falciparum
    • Sharma A., and Biswas S. Stage-specific cytosolic protein kinase C-like activity in human malarial parasite Plasmodium falciparum. Ind. J. Biochem. Biophys. 42 (2005) 145-151
    • (2005) Ind. J. Biochem. Biophys. , vol.42 , pp. 145-151
    • Sharma, A.1    Biswas, S.2
  • 27
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith T.F., and Waterman M.S. Identification of common molecular subsequences. J. Mol. Biol. 147 (1981) 195-197
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 28
    • 0020529536 scopus 로고
    • Purification and characterization of bovine hepatic uroporphyrinogen decarboxylase
    • Straka J.G., and Kushner J.P. Purification and characterization of bovine hepatic uroporphyrinogen decarboxylase. Biochemistry 22 (1983) 4664-4672
    • (1983) Biochemistry , vol.22 , pp. 4664-4672
    • Straka, J.G.1    Kushner, J.P.2
  • 29
    • 0026785410 scopus 로고
    • De novo biosynthesis of haem offers a new chemotherapeutic target in the human malarial parasite
    • Surolia A., and Padmanaban G. De novo biosynthesis of haem offers a new chemotherapeutic target in the human malarial parasite. Biochem. Biophys. Res. Comm. 187 (1992) 744-750
    • (1992) Biochem. Biophys. Res. Comm. , vol.187 , pp. 744-750
    • Surolia, A.1    Padmanaban, G.2
  • 30
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 31
    • 3343010591 scopus 로고    scopus 로고
    • Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method
    • Tonkin C.J., van Dooren G.G., Spurck T.P., Struck N.S., Good R.T., Handman E., Cowman A.F., and McFadden G.J. Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method. Mol. Biochem. Parasitol. 137 (2004) 13-21
    • (2004) Mol. Biochem. Parasitol. , vol.137 , pp. 13-21
    • Tonkin, C.J.1    van Dooren, G.G.2    Spurck, T.P.3    Struck, N.S.4    Good, R.T.5    Handman, E.6    Cowman, A.F.7    McFadden, G.J.8
  • 32
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager W., and Jensen J.B. Human malaria parasites in continuous culture. Science 193 (1976) 673-675
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 33
  • 34
    • 0037108901 scopus 로고    scopus 로고
    • Involvement of δ-aminolevulinate synthase encoded by the parasite gene in de novo heme synthesis by Plasmodium falciparum
    • Varadharajan S., Dhanasekaran S., Bonday Z.Q., Rangarajan P.N., and Padmanaban G. Involvement of δ-aminolevulinate synthase encoded by the parasite gene in de novo heme synthesis by Plasmodium falciparum. Biochem. J. 367 (2002) 321-327
    • (2002) Biochem. J. , vol.367 , pp. 321-327
    • Varadharajan, S.1    Dhanasekaran, S.2    Bonday, Z.Q.3    Rangarajan, P.N.4    Padmanaban, G.5
  • 36
    • 0028566384 scopus 로고
    • Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction
    • Weiner M.P., Costa G.L., Schoettlin W., Cline J., Mathur E., and Bauer J.C. Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction. Gene 151 (1994) 119-123
    • (1994) Gene , vol.151 , pp. 119-123
    • Weiner, M.P.1    Costa, G.L.2    Schoettlin, W.3    Cline, J.4    Mathur, E.5    Bauer, J.C.6
  • 37
    • 0032079342 scopus 로고    scopus 로고
    • Crystal structure of human uroporphyrinogen decarboxylase
    • Whitby F.G., Phillips J.D., Kushner J.P., and Hill C.P. Crystal structure of human uroporphyrinogen decarboxylase. EMBO J. 17 (1998) 2463-2471
    • (1998) EMBO J. , vol.17 , pp. 2463-2471
    • Whitby, F.G.1    Phillips, J.D.2    Kushner, J.P.3    Hill, C.P.4
  • 38
    • 0029670146 scopus 로고    scopus 로고
    • Characterization of the δ-aminolevulinate synthase gene homologue from P. falciparum
    • Wilson C.M., Smith A.B., and Baylon R.V. Characterization of the δ-aminolevulinate synthase gene homologue from P. falciparum. Mol. Biochem. Parasitol. 75 (1996) 271-276
    • (1996) Mol. Biochem. Parasitol. , vol.75 , pp. 271-276
    • Wilson, C.M.1    Smith, A.B.2    Baylon, R.V.3
  • 39
    • 13444301270 scopus 로고    scopus 로고
    • Parasite plastids: approaching the end game
    • Wilson R.J. Parasite plastids: approaching the end game. Biol. Rev. 80 (2005) 129-153
    • (2005) Biol. Rev. , vol.80 , pp. 129-153
    • Wilson, R.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.