메뉴 건너뛰기




Volumn 5, Issue 7, 2013, Pages 769-779

Targeting the vitamin biosynthesis pathways for the treatment of malaria

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); ANTIMALARIAL AGENT; COCARBOXYLASE; FOLIC ACID ANTAGONIST; GLYCERALDEHYDE 3 PHOSPHATE; OXOGLUTARATE DEHYDROGENASE; PYRIDOXAL; PYRIDOXAL 5 PHOSPHATE; PYRIDOXAMINE; PYRIDOXINE; PYRIMETHAMINE; PYRIMETHAMINE PLUS SULFADOXINE; PYRUVATE DEHYDROGENASE; RIBOSE 5 PHOSPHATE; SULFANILAMIDE DERIVATIVE; THIAMINE; THIAMINE PHOSPHATE; THIAMINE TRIPHOSPHATE; TRANSCRIPTION FACTOR PDX 1;

EID: 84877623608     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.13.43     Document Type: Review
Times cited : (10)

References (67)
  • 1
    • 84871041813 scopus 로고    scopus 로고
    • Antimalarial drug discovery: Where next?
    • Burrows JN. Antimalarial drug discovery: where next? Future Med. Chem. 4(18), 2233-2235
    • Future Med. Chem. , vol.4 , Issue.18 , pp. 2233-2235
    • Burrows, J.N.1
  • 2
    • 84856408211 scopus 로고    scopus 로고
    • World Health Organisation WHO Press, Geneva, Switzerland
    • World Health Organisation. World Malaria Report 2011. WHO Press, Geneva, Switzerland (2012).
    • (2012) World Malaria Report 2011
  • 3
    • 77957962900 scopus 로고    scopus 로고
    • The emerging of the fifth malaria parasite (Plasmodium knowlesi): A public health concern?
    • Sabbatani S, Fiorino S, Manfredi R. The emerging of the fifth malaria parasite (Plasmodium knowlesi): a public health concern? Braz. J. Infect. Dis. 14(3), 299-309 (2010).
    • (2010) Braz. J. Infect. Dis. , vol.14 , Issue.3 , pp. 299-309
    • Sabbatani, S.1    Fiorino, S.2    Manfredi, R.3
  • 4
    • 41849125318 scopus 로고    scopus 로고
    • Malaria: Progress, perils, and prospects for eradication
    • Greenwood BM, Fidock DA, Kyle DE, et al. Malaria: progress, perils, and prospects for eradication. J. Clin. Invest. 118(4), 1266-1276 (2008).
    • (2008) J. Clin. Invest. , vol.118 , Issue.4 , pp. 1266-1276
    • Greenwood, B.M.1    Fidock, D.A.2    Kyle, D.E.3
  • 5
    • 84871053194 scopus 로고    scopus 로고
    • Ferrous iron-dependent delivery of therapeutic agents to the malaria parasite
    • Mahajan SS, Gut J, Rosenthal PJ, Renslo AR. Ferrous iron-dependent delivery of therapeutic agents to the malaria parasite. Future Med. Chem. 4(18), 2241-2249 (2012).
    • (2012) Future Med. Chem. , vol.4 , Issue.18 , pp. 2241-2249
    • Mahajan, S.S.1    Gut, J.2    Rosenthal, P.J.3    Renslo, A.R.4
  • 6
    • 36849052939 scopus 로고    scopus 로고
    • Impact of artemisinin-based combination therapy and insecticide-treated nets on malaria burden in Zanzibar
    • Bhattarai A, Ali AS, Kachur SP, et al. Impact of artemisinin-based combination therapy and insecticide-treated nets on malaria burden in Zanzibar. PLoS Med. 4(11), e309 (2007).
    • (2007) PLoS Med. , vol.4 , Issue.11
    • Bhattarai, A.1    Ali, A.S.2    Kachur, S.P.3
  • 7
    • 68049123592 scopus 로고    scopus 로고
    • Artemisinin resistance in Plasmodium falciparum malaria
    • Dondorp AM, Nosten F, Yi P, et al. Artemisinin resistance in Plasmodium falciparum malaria. N. Engl. J. Med. 361(5), 455-467 (2009).
    • (2009) N. Engl. J. Med. , vol.361 , Issue.5 , pp. 455-467
    • Dondorp, A.M.1    Nosten, F.2    Yi, P.3
  • 8
    • 78650486233 scopus 로고    scopus 로고
    • Antimalarial drugs: Modes of action and mechanisms of parasite resistance
    • Müller IB, Hyde JE. Antimalarial drugs: modes of action and mechanisms of parasite resistance. Future Microbiol. 5(12), 1857-1873 (2010).
    • (2010) Future Microbiol. , vol.5 , Issue.12 , pp. 1857-1873
    • Müller, I.B.1    Hyde, J.E.2
  • 9
    • 19444371029 scopus 로고    scopus 로고
    • Comparative folate metabolism in humans and malaria parasites (part I): Pointers for malaria treatment from cancer chemotherapy
    • Nzila A, Ward SA, Marsh K, Sims PF, Hyde JE. Comparative folate metabolism in humans and malaria parasites (part I): pointers for malaria treatment from cancer chemotherapy. Trends Parasitol. 21(6), 292-298 (2005).
    • (2005) Trends Parasitol. , vol.21 , Issue.6 , pp. 292-298
    • Nzila, A.1    Ward, S.A.2    Marsh, K.3    Sims, P.F.4    Hyde, J.E.5
  • 10
    • 26844494887 scopus 로고    scopus 로고
    • Drug-resistant malaria
    • Hyde JE. Drug-resistant malaria. Trends Parasitol. 21(11), 494-498 (2005).
    • (2005) Trends Parasitol. , vol.21 , Issue.11 , pp. 494-498
    • Hyde, J.E.1
  • 11
    • 34548409606 scopus 로고    scopus 로고
    • Drug-resistant malaria - An insight
    • Hyde JE. Drug-resistant malaria - an insight. FEBS J. 274(18), 4688-4698 (2007).
    • (2007) FEBS J. , vol.274 , Issue.18 , pp. 4688-4698
    • Hyde, J.E.1
  • 12
    • 72149097595 scopus 로고    scopus 로고
    • Vitamin B metabolism in Plasmodium falciparum as a source of drug targets
    • Müller IB, Hyde JE, Wrenger C. Vitamin B metabolism in Plasmodium falciparum as a source of drug targets. Trends Parasitol. 26(1), 35-43 (2010).
    • (2010) Trends Parasitol. , vol.26 , Issue.1 , pp. 35-43
    • Müller, I.B.1    Hyde, J.E.2    Wrenger, C.3
  • 13
    • 0013524391 scopus 로고
    • The influence of antimalarial drugs on nucleic acid synthesis in Plasmodium gallinaceum and Plasmodium berghei
    • Schellenberg KA, Coatney GR. The influence of antimalarial drugs on nucleic acid synthesis in Plasmodium gallinaceum and Plasmodium berghei. Biochem. Pharmacol. 6, 143-152 (1961).
    • (1961) Biochem. Pharmacol. , vol.6 , pp. 143-152
    • Schellenberg, K.A.1    Coatney, G.R.2
  • 14
    • 84455169978 scopus 로고    scopus 로고
    • The molecular basis of folate salvage in Plasmodium falciparum: Characterization of two folate transporters
    • Salcedo-Sora JE, Ochong E, Beveridge S, et al. The molecular basis of folate salvage in Plasmodium falciparum: characterization of two folate transporters. J. Biol. Chem. 286(52), 44659-44668 (2011).
    • (2011) J. Biol. Chem. , vol.286 , Issue.52 , pp. 44659-44668
    • Salcedo-Sora, J.E.1    Ochong, E.2    Beveridge, S.3
  • 15
    • 55449133690 scopus 로고    scopus 로고
    • Adaptive copy number evolution in malaria parasites
    • Nair S, Miller B, Barends M, et al. Adaptive copy number evolution in malaria parasites. PLoS Genet. 4(10), e1000243 (2008).
    • (2008) PLoS Genet. , vol.4 , Issue.10
    • Nair, S.1    Miller, B.2    Barends, M.3
  • 16
    • 37749020557 scopus 로고    scopus 로고
    • An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites
    • Dittrich S, Mitchell SL, Blagborough AM, et al. An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites. Mol. Microbiol. 67(3), 609-618 (2008).
    • (2008) Mol. Microbiol. , vol.67 , Issue.3 , pp. 609-618
    • Dittrich, S.1    Mitchell, S.L.2    Blagborough, A.M.3
  • 17
    • 0035060361 scopus 로고    scopus 로고
    • Mode of action and mechanisms of resistance for antimalarial drugs
    • Olliaro P. Mode of action and mechanisms of resistance for antimalarial drugs. Pharmacol. Ther. 89(2), 207-219 (2001).
    • (2001) Pharmacol. Ther. , vol.89 , Issue.2 , pp. 207-219
    • Olliaro, P.1
  • 18
    • 42049115684 scopus 로고    scopus 로고
    • Effect of folate derivatives on the activity of antifolate drugs used against malaria and cancer
    • Nduati E, Diriye A, Ommeh S, et al. Effect of folate derivatives on the activity of antifolate drugs used against malaria and cancer. Parasitol. Res. 102(6), 1227-1234 (2008).
    • (2008) Parasitol. Res. , vol.102 , Issue.6 , pp. 1227-1234
    • Nduati, E.1    Diriye, A.2    Ommeh, S.3
  • 19
    • 0019293872 scopus 로고
    • Studies on the chemotherapy of human opisthorchiasis in Thailand: I. Clinical trial of praziquantel
    • Bunnag D, Harinasuta T. Studies on the chemotherapy of human opisthorchiasis in Thailand: I. Clinical trial of praziquantel. Southeast Asian J. Trop. Med. Public Health 11(4), 528-531 (1980).
    • (1980) Southeast Asian J. Trop. Med. Public Health , vol.11 , Issue.4 , pp. 528-531
    • Bunnag, D.1    Harinasuta, T.2
  • 21
    • 0042368854 scopus 로고    scopus 로고
    • Thiamine triphosphate and thiamine triphosphatase activities: From bacteria to mammals
    • Makarchikov AF, Lakaye B, Gulyai IE, et al. Thiamine triphosphate and thiamine triphosphatase activities: from bacteria to mammals. Cell Mol. Life Sci. 60(7), 1477-1488 (2003).
    • (2003) Cell Mol. Life Sci. , vol.60 , Issue.7 , pp. 1477-1488
    • Makarchikov, A.F.1    Lakaye, B.2    Gulyai, I.E.3
  • 23
    • 0024155397 scopus 로고
    • Thiamine and the brain
    • Haas RH. Thiamine and the brain. Annu. Rev. Nutr. 8, 483-515 (1988).
    • (1988) Annu. Rev. Nutr. , vol.8 , pp. 483-515
    • Haas, R.H.1
  • 25
    • 0032901233 scopus 로고    scopus 로고
    • Thiamin biosynthesis in prokaryotes
    • Begley TP, Downs DM, Ealick SE, et al. Thiamin biosynthesis in prokaryotes. Arch Microbiol. 171(5), 293-300 (1999).
    • (1999) Arch Microbiol. , vol.171 , Issue.5 , pp. 293-300
    • Begley, T.P.1    Downs, D.M.2    Ealick, S.E.3
  • 26
    • 0037804259 scopus 로고    scopus 로고
    • The THI5 gene family of Saccharomyces cerevisiae: Distribution of homologues among the hemiascomycetes and functional redundancy in the aerobic biosynthesis of thiamin from pyridoxine
    • Wightman R, Meacock PA. The THI5 gene family of Saccharomyces cerevisiae: distribution of homologues among the hemiascomycetes and functional redundancy in the aerobic biosynthesis of thiamin from pyridoxine. Microbiology 149(Pt 6), 1447-1460 (2003).
    • (2003) Microbiology , vol.149 , Issue.PART 6 , pp. 1447-1460
    • Wightman, R.1    Meacock, P.A.2
  • 27
    • 30644456408 scopus 로고    scopus 로고
    • Vitamin B1 de novo synthesis in the human malaria parasite Plasmodium falciparum depends on external provision of 4-amino-5- hydroxymethyl-2- methylpyrimidine
    • Wrenger C, Eschbach ML, Müller IB, Laun NP, Begley TP, Walter RD. Vitamin B1 de novo synthesis in the human malaria parasite Plasmodium falciparum depends on external provision of 4-amino-5- hydroxymethyl-2-methylpyrimidine. Biol. Chem. 387(1), 41-51 (2006).
    • (2006) Biol. Chem. , vol.387 , Issue.1 , pp. 41-51
    • Wrenger, C.1    Eschbach, M.L.2    Müller, I.B.3    Laun, N.P.4    Begley, T.P.5    Walter, R.D.6
  • 28
    • 0021909963 scopus 로고
    • Nutritional requirements of Plasmodium falciparum in culture. I. Exogenously supplied dialyzable components necessary for continuous growth
    • Divo AA, Geary TG, Davis NL, Jensen JB. Nutritional requirements of Plasmodium falciparum in culture. I. Exogenously supplied dialyzable components necessary for continuous growth. J. Protozool. 32(1), 59-64 (1985).
    • (1985) J. Protozool. , vol.32 , Issue.1 , pp. 59-64
    • Divo, A.A.1    Geary, T.G.2    Davis, N.L.3    Jensen, J.B.4
  • 29
    • 0032564596 scopus 로고    scopus 로고
    • Overexpression, purification and characterization of two pyrimidine kinases involved in the biosynthesis of thiamin: 4-amino-5-hydroxymethyl-2- methylpyrimidine kinase and 4-amino-5- hydroxymethyl-2-methylpyrimidine phosphate kinase
    • Reddick JJ, Kinsland C, Nicewonger R, et al. Overexpression, purification and characterization of two pyrimidine kinases involved in the biosynthesis of thiamin: 4-amino-5-hydroxymethyl-2- methylpyrimidine kinase and 4-amino-5- hydroxymethyl-2-methylpyrimidine phosphate kinase. Tetrahedron 54(52), 159873-115991 (1998).
    • (1998) Tetrahedron , vol.54 , Issue.52 , pp. 159873-115991
    • Reddick, J.J.1    Kinsland, C.2    Nicewonger, R.3
  • 30
    • 33847055382 scopus 로고    scopus 로고
    • Vitamin and cofactor biosynthesis pathways in Plasmodium and other apicomplexan parasites
    • Müller S, Kappes B. Vitamin and cofactor biosynthesis pathways in Plasmodium and other apicomplexan parasites. Trends Parasitol. 23(3), 112-121 (2007).
    • (2007) Trends Parasitol. , vol.23 , Issue.3 , pp. 112-121
    • Müller, S.1    Kappes, B.2
  • 31
    • 0030902603 scopus 로고    scopus 로고
    • Characterization of the Bacillus subtilis ThiC operon involved in thiamine biosynthesis
    • Zhang Y, Taylor SV, Chiu HJ, Begley TP. Characterization of the Bacillus subtilis ThiC operon involved in thiamine biosynthesis. J. Bacteriol. 179(9), 3030-3035 (1997).
    • (1997) J. Bacteriol. , vol.179 , Issue.9 , pp. 3030-3035
    • Zhang, Y.1    Taylor, S.V.2    Chiu, H.J.3    Begley, T.P.4
  • 32
    • 0032537591 scopus 로고    scopus 로고
    • Thiamin metabolism and thiamin diphosphate-dependent enzymes in the yeast Saccharomyces cerevisiae: Genetic regulation
    • Hohmann S, Meacock PA. Thiamin metabolism and thiamin diphosphate-dependent enzymes in the yeast Saccharomyces cerevisiae: genetic regulation. Biochim. Biophys. Acta 1385(2), 201-219 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1385 , Issue.2 , pp. 201-219
    • Hohmann, S.1    Meacock, P.A.2
  • 33
    • 0037715424 scopus 로고    scopus 로고
    • Systematic discovery of analogous enzymes in thiamin biosynthesis
    • Morett E, Korbel JO, Rajan E, et al. Systematic discovery of analogous enzymes in thiamin biosynthesis. Nat. Biotechnol. 21(7), 790-795 (2003).
    • (2003) Nat. Biotechnol. , vol.21 , Issue.7 , pp. 790-795
    • Morett, E.1    Korbel, J.O.2    Rajan, E.3
  • 34
    • 0035964325 scopus 로고    scopus 로고
    • Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase
    • Peapus DH, Chiu HJ, Campobasso N, Reddick JJ, Begley TP, Ealick SE. Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase. Biochemistry 40(34), 10103-10114 (2001).
    • (2001) Biochemistry , vol.40 , Issue.34 , pp. 10103-10114
    • Peapus, D.H.1    Chiu, H.J.2    Campobasso, N.3    Reddick, J.J.4    Begley, T.P.5    Ealick, S.E.6
  • 35
    • 33751509429 scopus 로고    scopus 로고
    • The human malaria parasite Plasmodium falciparum expresses an atypical N-terminally extended pyrophosphokinase with specificity for thiamine
    • Eschbach ML, Müller IB, Gilberger TW, Walter RD, Wrenger C. The human malaria parasite Plasmodium falciparum expresses an atypical N-terminally extended pyrophosphokinase with specificity for thiamine. Biol. Chem. 387(12), 1583-1591 (2006).
    • (2006) Biol. Chem. , vol.387 , Issue.12 , pp. 1583-1591
    • Eschbach, M.L.1    Müller, I.B.2    Gilberger, T.W.3    Walter, R.D.4    Wrenger, C.5
  • 36
    • 38049186917 scopus 로고    scopus 로고
    • Filling the gap of intracellular dephosphorylation in the Plasmodium falciparum vitamin B1 biosynthesis
    • Knöckel J, Bergmann B, Müller IB, Rathaur S, Walter RD, Wrenger C. Filling the gap of intracellular dephosphorylation in the Plasmodium falciparum vitamin B1 biosynthesis. Mol. Biochem. Parasitol. 157(2), 241-243 (2008).
    • (2008) Mol. Biochem. Parasitol. , vol.157 , Issue.2 , pp. 241-243
    • Knöckel, J.1    Bergmann, B.2    Müller, I.B.3    Rathaur, S.4    Walter, R.D.5    Wrenger, C.6
  • 37
    • 6344235639 scopus 로고    scopus 로고
    • A genetic screen for the identification of thiamin metabolic genes
    • Lawhorn BG, Gerdes SY, Begley TP. A genetic screen for the identification of thiamin metabolic genes. J. Biol. Chem. 279(42), 43555-43559 (2004).
    • (2004) J. Biol. Chem. , vol.279 , Issue.42 , pp. 43555-43559
    • Lawhorn, B.G.1    Gerdes, S.Y.2    Begley, T.P.3
  • 38
    • 0142186241 scopus 로고    scopus 로고
    • A genomic overview of pyridoxal-phosphate-dependent enzymes
    • Percudani R, Peracchi A. A genomic overview of pyridoxal-phosphate- dependent enzymes. EMBO Rep. 4(9), 850-854 (2003).
    • (2003) EMBO Rep. , vol.4 , Issue.9 , pp. 850-854
    • Percudani, R.1    Peracchi, A.2
  • 39
    • 79960175330 scopus 로고    scopus 로고
    • A novel approach to inhibit intracellular vitamin B6-dependent enzymes: Proof of principle with human and plasmodium ornithine decarboxylase and human histidine decarboxylase
    • Wu F, Christen P, Gehring H. A novel approach to inhibit intracellular vitamin B6-dependent enzymes: proof of principle with human and plasmodium ornithine decarboxylase and human histidine decarboxylase. FASEB J. 25(7), 2109-2122 (2011).
    • (2011) FASEB J. , vol.25 , Issue.7 , pp. 2109-2122
    • Wu, F.1    Christen, P.2    Gehring, H.3
  • 40
    • 59649110686 scopus 로고    scopus 로고
    • Structural requirements for novel coenzyme-substrate derivatives to inhibit intracellular ornithine decarboxylase and cell proliferation
    • Wu F, Gehring H. Structural requirements for novel coenzyme-substrate derivatives to inhibit intracellular ornithine decarboxylase and cell proliferation. FASEB J. 23(2), 565-574 (2009).
    • (2009) FASEB J. , vol.23 , Issue.2 , pp. 565-574
    • Wu, F.1    Gehring, H.2
  • 41
    • 35148883429 scopus 로고    scopus 로고
    • Two independent routes of de novo vitamin B6 biosynthesis: Not that different after all
    • Fitzpatrick TB, Amrhein N, Kappes B, Macheroux P, Tews I, Raschle T. Two independent routes of de novo vitamin B6 biosynthesis: not that different after all. Biochem. J. 407(1), 1-13 (2007).
    • (2007) Biochem. J. , vol.407 , Issue.1 , pp. 1-13
    • Fitzpatrick, T.B.1    Amrhein, N.2    Kappes, B.3    Macheroux, P.4    Tews, I.5    Raschle, T.6
  • 42
    • 0024730183 scopus 로고
    • Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12
    • Roa BB, Connolly DM, Winkler ME. Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12. J. Bacteriol. 171(9), 4767-4777 (1989).
    • (1989) J. Bacteriol. , vol.171 , Issue.9 , pp. 4767-4777
    • Roa, B.B.1    Connolly, D.M.2    Winkler, M.E.3
  • 43
    • 0026538262 scopus 로고
    • Suppression of insertions in the complex pdxJ operon of Escherichia coli K-12 by lon and other mutations
    • Lam HM, Tancula E, Dempsey WB, Winkler ME. Suppression of insertions in the complex pdxJ operon of Escherichia coli K-12 by lon and other mutations. J. Bacteriol. 174(5), 1554-1567 (1992).
    • (1992) J. Bacteriol. , vol.174 , Issue.5 , pp. 1554-1567
    • Lam, H.M.1    Tancula, E.2    Dempsey, W.B.3    Winkler, M.E.4
  • 46
    • 0031795758 scopus 로고    scopus 로고
    • The highly conserved, coregulated SNO and SNZ gene families in Saccharomyces cerevisiae respond to nutrient limitation
    • Padilla PA, Fuge EK, Crawford ME, Errett A, Werner-Washburne M. The highly conserved, coregulated SNO and SNZ gene families in Saccharomyces cerevisiae respond to nutrient limitation. J. Bacteriol. 180(21), 5718-5726 (1998).
    • (1998) J. Bacteriol. , vol.180 , Issue.21 , pp. 5718-5726
    • Padilla, P.A.1    Fuge, E.K.2    Crawford, M.E.3    Errett, A.4    Werner-Washburne, M.5
  • 47
    • 0033551830 scopus 로고    scopus 로고
    • The extremely conserved pyroA gene of Aspergillus nidulans is required for pyridoxine synthesis and is required indirectly for resistance to photosensitizers
    • Osmani AH, May GS, Osmani SA. The extremely conserved pyroA gene of Aspergillus nidulans is required for pyridoxine synthesis and is required indirectly for resistance to photosensitizers. J. Biol. Chem. 274(33), 23565-23569 (1999).
    • (1999) J. Biol. Chem. , vol.274 , Issue.33 , pp. 23565-23569
    • Osmani, A.H.1    May, G.S.2    Osmani, S.A.3
  • 48
    • 0032015703 scopus 로고    scopus 로고
    • SOR1, a gene required for photosensitizer and singlet oxygen resistance in Cercospora fungi, is highly conserved in divergent organisms
    • Ehrenshaft M, Jenns AE, Chung KR, Daub ME. SOR1, a gene required for photosensitizer and singlet oxygen resistance in Cercospora fungi, is highly conserved in divergent organisms. Mol. Cell 1(4), 603-609 (1998).
    • (1998) Mol. Cell , vol.1 , Issue.4 , pp. 603-609
    • Ehrenshaft, M.1    Jenns, A.E.2    Chung, K.R.3    Daub, M.E.4
  • 49
    • 0033529936 scopus 로고    scopus 로고
    • A highly conserved sequence is a novel gene involved in de novo vitamin B6 biosynthesis
    • Ehrenshaft M, Bilski P, Li MY, Chignell CF, Daub ME. A highly conserved sequence is a novel gene involved in de novo vitamin B6 biosynthesis. Proc. Natl Acad. Sci. USA 96(16), 9374-9378 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , Issue.16 , pp. 9374-9378
    • Ehrenshaft, M.1    Bilski, P.2    Li, M.Y.3    Chignell, C.F.4    Daub, M.E.5
  • 50
    • 1142298586 scopus 로고    scopus 로고
    • Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5́-phosphate biosynthesis
    • Belitsky BR. Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5́-phosphate biosynthesis. J. Bacteriol. 186(4), 1191-1196 (2004).
    • (2004) J. Bacteriol. , vol.186 , Issue.4 , pp. 1191-1196
    • Belitsky, B.R.1
  • 51
    • 25444433588 scopus 로고    scopus 로고
    • On the two components of pyridoxal 5́-phosphate synthase from Bacillus subtilis
    • Raschle T, Amrhein N, Fitzpatrick TB. On the two components of pyridoxal 5́-phosphate synthase from Bacillus subtilis. J. Biol. Chem. 280(37), 32291-32300 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.37 , pp. 32291-32300
    • Raschle, T.1    Amrhein, N.2    Fitzpatrick, T.B.3
  • 52
    • 15744377644 scopus 로고    scopus 로고
    • Reconstitution and biochemical characterization of a new pyridoxal-5́-phosphate biosynthetic pathway
    • Burns KE, Xiang Y, Kinsland CL, Mclafferty FW, Begley TP. Reconstitution and biochemical characterization of a new pyridoxal-5́-phosphate biosynthetic pathway. J. Am. Chem. Soc. 127(11), 3682-3683 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.11 , pp. 3682-3683
    • Burns, K.E.1    Xiang, Y.2    Kinsland, C.L.3    McLafferty, F.W.4    Begley, T.P.5
  • 53
    • 33845928807 scopus 로고    scopus 로고
    • Structure of a bacterial pyridoxal 5́-phosphate synthase complex
    • Strohmeier M, Raschle T, Mazurkiewicz J, et al. Structure of a bacterial pyridoxal 5́-phosphate synthase complex. Proc. Natl Acad. Sci. USA 103(51), 19284-19289 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , Issue.51 , pp. 19284-19289
    • Strohmeier, M.1    Raschle, T.2    Mazurkiewicz, J.3
  • 54
    • 1642453681 scopus 로고    scopus 로고
    • Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5́-phosphate biosynthesis
    • Bauer JA, Bennett EM, Begley TP, Ealick SE. Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5́- phosphate biosynthesis. J. Biol. Chem. 279(4), 2704-2711 (2004).
    • (2004) J. Biol. Chem. , vol.279 , Issue.4 , pp. 2704-2711
    • Bauer, J.A.1    Bennett, E.M.2    Begley, T.P.3    Ealick, S.E.4
  • 55
    • 23044515503 scopus 로고    scopus 로고
    • A new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase
    • Zhu J, Burgner JW, Harms E, Belitsky BR, Smith JL. A new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase. J. Biol. Chem. 280(30), 27914-27923 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.30 , pp. 27914-27923
    • Zhu, J.1    Burgner, J.W.2    Harms, E.3    Belitsky, B.R.4    Smith, J.L.5
  • 56
    • 33845468647 scopus 로고    scopus 로고
    • Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima
    • Zein F, Zhang Y, Kang YN, Burns K, Begley TP, Ealick SE. Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima. Biochemistry 45(49), 14609-14620 (2006).
    • (2006) Biochemistry , vol.45 , Issue.49 , pp. 14609-14620
    • Zein, F.1    Zhang, Y.2    Kang, Y.N.3    Burns, K.4    Begley, T.P.5    Ealick, S.E.6
  • 57
    • 10644295471 scopus 로고    scopus 로고
    • The methylerythritol phosphate pathway is functionally active in all intraerythrocytic stages of Plasmodium falciparum
    • Cassera MB, Gozzo Fc, D'alexandri Fl, et al. The methylerythritol phosphate pathway is functionally active in all intraerythrocytic stages of Plasmodium falciparum. J. Biol. Chem. 279(50), 51749-51759 (2004).
    • (2004) J. Biol. Chem. , vol.279 , Issue.50 , pp. 51749-51759
    • Cassera, M.B.1    Gozzo, F.C.2    D'Alexandri, F.L.3
  • 58
    • 14044255850 scopus 로고    scopus 로고
    • Analysis of the vitamin B6 biosynthesis pathway in the human malaria parasite Plasmodium falciparum
    • Wrenger C, Eschbach ML, Müller IB, Warnecke D, Walter RD. Analysis of the vitamin B6 biosynthesis pathway in the human malaria parasite Plasmodium falciparum. J. Biol. Chem. 280(7), 5242-5248 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.7 , pp. 5242-5248
    • Wrenger, C.1    Eschbach, M.L.2    Müller, I.B.3    Warnecke, D.4    Walter, R.D.5
  • 59
    • 33645646965 scopus 로고    scopus 로고
    • Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum: Biochemical and structural insights
    • Gengenbacher M, Fitzpatrick TB, Raschle T, et al. Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum: biochemical and structural insights. J. Biol. Chem. 281(6), 3633-3641 (2006).
    • (2006) J. Biol. Chem. , vol.281 , Issue.6 , pp. 3633-3641
    • Gengenbacher, M.1    Fitzpatrick, T.B.2    Raschle, T.3
  • 61
    • 4444359792 scopus 로고    scopus 로고
    • Redox and antioxidant systems of the malaria parasite Plasmodium falciparum
    • Müller S. Redox and antioxidant systems of the malaria parasite Plasmodium falciparum. Mol. Microbiol. 53(5), 1291-1305 (2004).
    • (2004) Mol. Microbiol. , vol.53 , Issue.5 , pp. 1291-1305
    • Müller, S.1
  • 63
    • 0036305476 scopus 로고    scopus 로고
    • The thioredoxin system of Plasmodium falciparum and other parasites
    • Rahlfs S, Schirmer RH, Becker K. The thioredoxin system of Plasmodium falciparum and other parasites. Cell Mol. Life Sci. 59(6), 1024-1041 (2002).
    • (2002) Cell Mol. Life Sci. , vol.59 , Issue.6 , pp. 1024-1041
    • Rahlfs, S.1    Schirmer, R.H.2    Becker, K.3
  • 64
    • 84859464651 scopus 로고    scopus 로고
    • The antioxidative effect of de novo generated vitamin B6 in Plasmodium falciparum validated by protein interference
    • Knöckel J, Müller IB, Butzloff S, Bergmann B, Walter RD, Wrenger C. The antioxidative effect of de novo generated vitamin B6 in Plasmodium falciparum validated by protein interference. Biochem. J. 443(2), 397-405 (2012).
    • (2012) Biochem. J. , vol.443 , Issue.2 , pp. 397-405
    • Knöckel, J.1    Müller, I.B.2    Butzloff, S.3    Bergmann, B.4    Walter, R.D.5    Wrenger, C.6
  • 65
    • 84870875476 scopus 로고    scopus 로고
    • Exploring inhibition of Pdx1, a component of the PLP synthase complex of the human malaria parasite Plasmodium falciparum
    • Reeksting SB, Müller IB, Burger PB, et al. Exploring inhibition of Pdx1, a component of the PLP synthase complex of the human malaria parasite Plasmodium falciparum. Biochem. J. 449(1), 175-187 (2013).
    • (2013) Biochem. J. , vol.449 , Issue.1 , pp. 175-187
    • Reeksting, S.B.1    Müller, I.B.2    Burger, P.B.3
  • 66
    • 84881156988 scopus 로고    scopus 로고
    • Poisoning pyridoxal 5-phosphate-dependent enzymes: A new strategy to target the malaria parasite Plasmodium falciparum
    • Müller IB, Wu F, Bergmann B, et al. Poisoning pyridoxal 5-phosphate-dependent enzymes: a new strategy to target the malaria parasite Plasmodium falciparum. PLoS ONE 4(2), e4406 (2009).
    • (2009) PLoS ONE , vol.4 , Issue.2
    • Müller, I.B.1    Wu, F.2    Bergmann, B.3
  • 67
    • 77952759972 scopus 로고    scopus 로고
    • Discovery of potent and selective inhibitors of Trypanosoma brucei ornithine decarboxylase
    • Smithson DC, Lee J, Shelat AA, Phillips MA, Guy RK. Discovery of potent and selective inhibitors of Trypanosoma brucei ornithine decarboxylase. J. Biol. Chem. 285(22), 16771-16781 (2008).
    • (2008) J. Biol. Chem. , vol.285 , Issue.22 , pp. 16771-16781
    • Smithson, D.C.1    Lee, J.2    Shelat, A.A.3    Phillips, M.A.4    Guy, R.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.