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Volumn 174, Issue 1, 2010, Pages 44-52

Protoporphyrinogen IX oxidase from Plasmodium falciparum is anaerobic and is localized to the mitochondrion

Author keywords

Anaerobic; Electron transport chain; Heme; Plasmodium falciparum; Protoporphyrinogen oxidase

Indexed keywords

ATOVAQUONE; CITRININ; MITOCHONDRIAL ENZYME; PROTOPORPHYRINOGEN OXIDASE; PYRIMIDINE;

EID: 77955842415     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2010.06.012     Document Type: Article
Times cited : (32)

References (42)
  • 1
    • 0026785410 scopus 로고
    • De novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite
    • Surolia N., Padmanaban G. De novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite. Biochem Biophys Res Commun 1992, 187:744-750.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 744-750
    • Surolia, N.1    Padmanaban, G.2
  • 2
    • 0030758361 scopus 로고    scopus 로고
    • Heme biosynthesis by the malarial parasite. Import of δ-aminolevulinate dehydrase from the host red cell
    • Bonday Z.Q., Taketani S., Gupta P.D., Padmanaban G. Heme biosynthesis by the malarial parasite. Import of δ-aminolevulinate dehydrase from the host red cell. J Biol Chem 1997, 272:21839-21846.
    • (1997) J Biol Chem , vol.272 , pp. 21839-21846
    • Bonday, Z.Q.1    Taketani, S.2    Gupta, P.D.3    Padmanaban, G.4
  • 3
    • 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., Padmanban G. Import of host δ-aminolevulinate dehydratase into the malarial parasite: identification of a new drug target. Nat Med 2000, 6:898-903.
    • (2000) Nat Med , vol.6 , pp. 898-903
    • Bonday, Z.Q.1    Dhanasekaran, S.2    Rangarajan, P.N.3    Padmanban, G.4
  • 4
    • 0037015614 scopus 로고    scopus 로고
    • Genome sequence of the human malaria parasite Plasmodium falciparum
    • Gardner M.J., Hall N., Fung E., et al. Genome sequence of the human malaria parasite Plasmodium falciparum. Nature 2002, 419:498-511.
    • (2002) Nature , vol.419 , pp. 498-511
    • Gardner, M.J.1    Hall, N.2    Fung, E.3
  • 5
    • 2342520626 scopus 로고    scopus 로고
    • Tropical infectious diseases: metabolic maps and functions of the Plasmodium falciparum apicoplast
    • Ralph S.A., van Dooren G.G., Waller R.F., et al. Tropical infectious diseases: metabolic maps and functions of the Plasmodium falciparum apicoplast. Nat Rev Microbiol 2004, 2:203-216.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 203-216
    • Ralph, S.A.1    van Dooren, G.G.2    Waller, R.F.3
  • 6
  • 7
    • 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., Wilson R.J. Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum. Protist 2004, 155:117-125.
    • (2004) Protist , vol.155 , pp. 117-125
    • Sato, S.1    Clough, B.2    Coates, L.3    Wilson, R.J.4
  • 8
    • 13444301270 scopus 로고    scopus 로고
    • Parasite plastids: approaching the endgame
    • Wilson R.J. Parasite plastids: approaching the endgame. Biol Rev 2005, 80:129-153.
    • (2005) Biol Rev , vol.80 , pp. 129-153
    • Wilson, R.J.1
  • 9
    • 35348914343 scopus 로고    scopus 로고
    • An alternative model for heme biosynthesis in the malarial parasite
    • Padmanaban G., Nagaraj V.A., Rangarajan P.N. An alternative model for heme biosynthesis in the malarial parasite. Trends Biochem Sci 2007, 32:443-449.
    • (2007) Trends Biochem Sci , vol.32 , pp. 443-449
    • Padmanaban, G.1    Nagaraj, V.A.2    Rangarajan, P.N.3
  • 10
    • 0029670146 scopus 로고    scopus 로고
    • Characterization of the δ aminolevulinate synthase gene homologue in P. falciparum
    • Wilson C.M., Smith A.B., Baylon R.V. Characterization of the δ aminolevulinate synthase gene homologue in P. falciparum. Mol Biochem Parasitol 1996, 75:271-276.
    • (1996) Mol Biochem Parasitol , vol.75 , pp. 271-276
    • Wilson, C.M.1    Smith, A.B.2    Baylon, R.V.3
  • 11
    • 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., Padmanaban G. Involvement of δ-aminolevulinate synthase encoded by the parasite gene in de novo heme synthesis by Plasmodium falciparum. Biochem J 2002, 367:321-327.
    • (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
  • 12
    • 1342325384 scopus 로고    scopus 로고
    • δ-Aminolevulinic acid dehydratase from Plasmodium falciparum: indigenous versus imported
    • Dhanasekaran S., Chandra N.R., Sagar B.K.C., Rangarajan P.N., Padmanaban G. δ-Aminolevulinic acid dehydratase from Plasmodium falciparum: indigenous versus imported. J Biol Chem 2004, 279:6934-6942.
    • (2004) J Biol Chem , vol.279 , pp. 6934-6942
    • Dhanasekaran, S.1    Chandra, N.R.2    Sagar, B.K.C.3    Rangarajan, P.N.4    Padmanaban, G.5
  • 14
    • 59749094634 scopus 로고    scopus 로고
    • Localization of Plasmodium falciparum uroporphyrinogen III decarboxylase of the heme-biosynthetic pathway in the apicoplast and characterization of its catalytic properties
    • Nagaraj V.A., Arumugam R., Chandra N.R., Prasad D., Rangarajan P.N., Padmanaban G. Localization of Plasmodium falciparum uroporphyrinogen III decarboxylase of the heme-biosynthetic pathway in the apicoplast and characterization of its catalytic properties. Int J Parasitol 2009, 39:559-568.
    • (2009) Int J Parasitol , vol.39 , pp. 559-568
    • Nagaraj, V.A.1    Arumugam, R.2    Chandra, N.R.3    Prasad, D.4    Rangarajan, P.N.5    Padmanaban, G.6
  • 15
    • 68749104332 scopus 로고    scopus 로고
    • Mitochondrial localization of functional ferrochelatase from Plasmodium falciparum
    • Nagaraj V.A., Prasad D., Rangarajan P.N., Padmanaban G. Mitochondrial localization of functional ferrochelatase from Plasmodium falciparum. Mol Biochem Parasitol 2009, 168:109-112.
    • (2009) Mol Biochem Parasitol , vol.168 , pp. 109-112
    • Nagaraj, V.A.1    Prasad, D.2    Rangarajan, P.N.3    Padmanaban, G.4
  • 16
    • 77951623241 scopus 로고    scopus 로고
    • Characterization of coproporphyrinogen III oxidase in Plasmodium falciparum cytosol
    • Nagaraj V.A., Prasad D., Arumugam R., Rangarajan P.N., Padmanaban G. Characterization of coproporphyrinogen III oxidase in Plasmodium falciparum cytosol. Parasitol Int 2010, 59:121-127.
    • (2010) Parasitol Int , vol.59 , pp. 121-127
    • Nagaraj, V.A.1    Prasad, D.2    Arumugam, R.3    Rangarajan, P.N.4    Padmanaban, G.5
  • 17
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous cultures
    • Trager W., Jensen J.B. Human malaria parasites in continuous cultures. Science 1976, 193:673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 18
    • 0022399476 scopus 로고
    • Oxidation of protoporphyrinogen in the obligate anaerobe Desulfovibrio gigas
    • Klem D.J., Barton L.L. Oxidation of protoporphyrinogen in the obligate anaerobe Desulfovibrio gigas. J Bacteriol 1985, 164:316-320.
    • (1985) J Bacteriol , vol.164 , pp. 316-320
    • Klem, D.J.1    Barton, L.L.2
  • 19
    • 0023445076 scopus 로고
    • Purification and properties of protoporphyrinogen oxidase from an anaerobic bacterium, Desulfovibrio gigas
    • Klem D.J., Barton L.L. Purification and properties of protoporphyrinogen oxidase from an anaerobic bacterium, Desulfovibrio gigas. J Bacteriol 1987, 169:5209-5215.
    • (1987) J Bacteriol , vol.169 , pp. 5209-5215
    • Klem, D.J.1    Barton, L.L.2
  • 20
    • 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., et al. Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method. Mol Biochem Parasitol 2004, 137:13-21.
    • (2004) Mol Biochem Parasitol , vol.137 , pp. 13-21
    • Tonkin, C.J.1    van Dooren, G.G.2    Spurck, T.P.3
  • 22
    • 0026592433 scopus 로고
    • Use of radioactive ethanolamine incorporation into phospholipids to assess in vitro antimalarial activity by the semiautomated microdilution technique
    • Elabbadi N., Ancelin M., Vial H.J. Use of radioactive ethanolamine incorporation into phospholipids to assess in vitro antimalarial activity by the semiautomated microdilution technique. Antimicrob Agents Chemother 1992, 36:50-55.
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 50-55
    • Elabbadi, N.1    Ancelin, M.2    Vial, H.J.3
  • 23
    • 0018606732 scopus 로고
    • Quantitative assessment of antimalarial activity in vitro by a semiautomated microdilution technique
    • Desjardins R.E., Canfield C.J., Haynes J.D., Chulay J.D. Quantitative assessment of antimalarial activity in vitro by a semiautomated microdilution technique. Antimicrob Agents Chemother 1979, 16:710-718.
    • (1979) Antimicrob Agents Chemother , vol.16 , pp. 710-718
    • Desjardins, R.E.1    Canfield, C.J.2    Haynes, J.D.3    Chulay, J.D.4
  • 24
    • 0030741944 scopus 로고    scopus 로고
    • Expression, purification, and characteristics of mammalian protoporphyrinogen oxidase
    • Dailey T.A., Dailey H.A. Expression, purification, and characteristics of mammalian protoporphyrinogen oxidase. Methods Enzymol 1997, 281:340-349.
    • (1997) Methods Enzymol , vol.281 , pp. 340-349
    • Dailey, T.A.1    Dailey, H.A.2
  • 25
    • 0026605065 scopus 로고
    • Site of action of the antimalarial hydroxynaphthoquinone, 2-[trans-4-(4'-chlorophenyl) cyclohexyl]-3-hydroxy-1,4-naphthoquinone (566C80)
    • Fry M., Pudney M. Site of action of the antimalarial hydroxynaphthoquinone, 2-[trans-4-(4'-chlorophenyl) cyclohexyl]-3-hydroxy-1,4-naphthoquinone (566C80). Biochem Pharmacol 1992, 43:1545-1553.
    • (1992) Biochem Pharmacol , vol.43 , pp. 1545-1553
    • Fry, M.1    Pudney, M.2
  • 26
    • 0002729324 scopus 로고    scopus 로고
    • Mitochondrial physiology as a target for atovaquone and other antimalarials
    • ASM Press, Washington, DC, I. Sherman (Ed.)
    • Vaidya A.B. Mitochondrial physiology as a target for atovaquone and other antimalarials. Malaria parasite biology, pathogenesis and protection 1998, 355-368. ASM Press, Washington, DC. I. Sherman (Ed.).
    • (1998) Malaria parasite biology, pathogenesis and protection , pp. 355-368
    • Vaidya, A.B.1
  • 27
    • 33847398001 scopus 로고    scopus 로고
    • Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum
    • Painter H.J., Morrisey J.M., Mather M.W., Vaidya A.B. Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum. Nature 2007, 446:88-91.
    • (2007) Nature , vol.446 , pp. 88-91
    • Painter, H.J.1    Morrisey, J.M.2    Mather, M.W.3    Vaidya, A.B.4
  • 28
    • 37549030520 scopus 로고    scopus 로고
    • Malaria-parasite mitochondrial dehydrogenases as drug targets: too early to write the obituary
    • Fisher N., Bray P.G., Ward S.A., Biagini G.A. Malaria-parasite mitochondrial dehydrogenases as drug targets: too early to write the obituary. Trends Parasitol 2008, 24:9-10.
    • (2008) Trends Parasitol , vol.24 , pp. 9-10
    • Fisher, N.1    Bray, P.G.2    Ward, S.A.3    Biagini, G.A.4
  • 29
    • 37249026903 scopus 로고    scopus 로고
    • Physiological states of Plasmodium falciparum in malaria-infected patients
    • Daily J.P., Scanfeld D., Pochet N., et al. Physiological states of Plasmodium falciparum in malaria-infected patients. Nature 2007, 450:1091-1095.
    • (2007) Nature , vol.450 , pp. 1091-1095
    • Daily, J.P.1    Scanfeld, D.2    Pochet, N.3
  • 30
    • 0032167638 scopus 로고    scopus 로고
    • The domain structure of protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides
    • Arnould S., Camadro J.-M. The domain structure of protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides. Proc Natl Acad Sci USA 1998, 95:10553-10558.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10553-10558
    • Arnould, S.1    Camadro, J.-M.2
  • 31
    • 0014740189 scopus 로고
    • Incorporation of radioactive precursors into DNA and RNA of Plasmodium knowlesi in vitro
    • Gutteridge W.E., Trigg P.I. Incorporation of radioactive precursors into DNA and RNA of Plasmodium knowlesi in vitro. J Protozool 1970, 17:89-96.
    • (1970) J Protozool , vol.17 , pp. 89-96
    • Gutteridge, W.E.1    Trigg, P.I.2
  • 32
    • 0026510588 scopus 로고
    • Molecular targets of 5-fluoroorotate in human malaria parasite, Plasmodium falciparum
    • Rathod P.K., Leffers N.P., Young R.D. Molecular targets of 5-fluoroorotate in human malaria parasite, Plasmodium falciparum. Antimicrob Agents Chemother 1992, 36:704-711.
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 704-711
    • Rathod, P.K.1    Leffers, N.P.2    Young, R.D.3
  • 33
    • 77953773127 scopus 로고    scopus 로고
    • Plasmodium dihydroorotate dehydrogenase; a promising target for novel anti-malarial therapy
    • Phillips M.A., Rathod P.K. Plasmodium dihydroorotate dehydrogenase; a promising target for novel anti-malarial therapy. Infect Disorders-Drug Targets 2010, 10:226-239.
    • (2010) Infect Disorders-Drug Targets , vol.10 , pp. 226-239
    • Phillips, M.A.1    Rathod, P.K.2
  • 34
    • 0032532619 scopus 로고    scopus 로고
    • Purification of and kinetic studies on a cloned protoporphyrinogen oxidase from the aerobic bacterium Bacillus subtilis
    • Corrigal A.V., Siziba K.B., Maneli M.H., Shephard E.G., Ziman M. Purification of and kinetic studies on a cloned protoporphyrinogen oxidase from the aerobic bacterium Bacillus subtilis. Arch Biochem Biophys 1998, 358:251-256.
    • (1998) Arch Biochem Biophys , vol.358 , pp. 251-256
    • Corrigal, A.V.1    Siziba, K.B.2    Maneli, M.H.3    Shephard, E.G.4    Ziman, M.5
  • 35
    • 53049102051 scopus 로고    scopus 로고
    • Metal ion substrate inhibition of ferrochelatase
    • Hunter G.A., Sampson M.P., Ferreira G.C. Metal ion substrate inhibition of ferrochelatase. J Biol Chem 2008, 283:23685-23691.
    • (2008) J Biol Chem , vol.283 , pp. 23685-23691
    • Hunter, G.A.1    Sampson, M.P.2    Ferreira, G.C.3
  • 36
    • 0037122942 scopus 로고    scopus 로고
    • Role of complex II in anaerobic respiration of the parasite mitochondria from Ascaris suum and Plasmodium falciparum
    • Kita K., Hirawake H., Miyadera H., Amino H., Takeo S. Role of complex II in anaerobic respiration of the parasite mitochondria from Ascaris suum and Plasmodium falciparum. Biochim Biophys Acta 2002, 1553:123-139.
    • (2002) Biochim Biophys Acta , vol.1553 , pp. 123-139
    • Kita, K.1    Hirawake, H.2    Miyadera, H.3    Amino, H.4    Takeo, S.5
  • 37
    • 0034656342 scopus 로고    scopus 로고
    • Succinate dehydrogenase in Plasmodium falciparum mitochondria: molecular characterization of the SDHA and SDHB genes for the catalytic subunits, the flavoprotein (Fp) and iron-sulfur (Ip) subunits
    • Takeo S., Kokaze A., Ng C.S., et al. Succinate dehydrogenase in Plasmodium falciparum mitochondria: molecular characterization of the SDHA and SDHB genes for the catalytic subunits, the flavoprotein (Fp) and iron-sulfur (Ip) subunits. Mol Biochem Parasitol 2000, 107:191-205.
    • (2000) Mol Biochem Parasitol , vol.107 , pp. 191-205
    • Takeo, S.1    Kokaze, A.2    Ng, C.S.3
  • 38
    • 70449094676 scopus 로고    scopus 로고
    • Identification of mitochondrial Complex II subunits SDH3 and SDH4 and ATP synthase subunits α and β in Plasmodium spp.
    • Mogi T., Kita K. Identification of mitochondrial Complex II subunits SDH3 and SDH4 and ATP synthase subunits α and β in Plasmodium spp. Mitochondrion 2009, 9:443-453.
    • (2009) Mitochondrion , vol.9 , pp. 443-453
    • Mogi, T.1    Kita, K.2
  • 39
    • 0035152999 scopus 로고    scopus 로고
    • Isolation of mitochondria from Plasmodium falciparum showing dihydroorotate dependent respiration
    • Takashima E., Takamiya S., Takeo S., et al. Isolation of mitochondria from Plasmodium falciparum showing dihydroorotate dependent respiration. Parasitol Int 2001, 50:273-278.
    • (2001) Parasitol Int , vol.50 , pp. 273-278
    • Takashima, E.1    Takamiya, S.2    Takeo, S.3
  • 40
    • 0038730358 scopus 로고    scopus 로고
    • Protonmotive pathways and mechanisms in the cytochrome bc1 complex
    • Hunte C., Palsdottir H., Trumpower B.L. Protonmotive pathways and mechanisms in the cytochrome bc1 complex. FEBS Lett 2003, 545:39-46.
    • (2003) FEBS Lett , vol.545 , pp. 39-46
    • Hunte, C.1    Palsdottir, H.2    Trumpower, B.L.3
  • 41
    • 0003766888 scopus 로고    scopus 로고
    • Atovaquone-proguanil combination in antimalarial chemotherapy
    • Humana Press, New Jersey, P.J. Rosenthal (Ed.)
    • Vaidya A.B. Atovaquone-proguanil combination in antimalarial chemotherapy. Mechanisms of action, resistance, and new directions in drug discovery 2001, 203-218. Humana Press, New Jersey. P.J. Rosenthal (Ed.).
    • (2001) Mechanisms of action, resistance, and new directions in drug discovery , pp. 203-218
    • Vaidya, A.B.1
  • 42
    • 0037154419 scopus 로고    scopus 로고
    • Characterization of the isoprenoid chain of coenzyme Q in Plasmodium falciparum
    • de Macedo C.S., Uhrig M.L., Kimura E.A., Katzin A.M. Characterization of the isoprenoid chain of coenzyme Q in Plasmodium falciparum. FEMS Microbiol Lett 2002, 207:13-20.
    • (2002) FEMS Microbiol Lett , vol.207 , pp. 13-20
    • de Macedo, C.S.1    Uhrig, M.L.2    Kimura, E.A.3    Katzin, A.M.4


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