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Volumn 7, Issue 1, 2011, Pages 41-52

Thiamin (vitamin B1) biosynthesis and regulation: A rich source of antimicrobial drug targets?

Author keywords

Drug targets; Mycobacterium tuberculosis; Riboswitch; Thiamin biosynthesis

Indexed keywords

BACTERIA (MICROORGANISMS); MYCOBACTERIUM TUBERCULOSIS;

EID: 79952467900     PISSN: 14492288     EISSN: None     Source Type: Journal    
DOI: 10.7150/ijbs.7.41     Document Type: Review
Times cited : (141)

References (90)
  • 1
    • 37349117988 scopus 로고    scopus 로고
    • Coenzyme A biosynthesis: An antimicrobial drug target
    • Spry C, Kirk K., and Saliba K.J. Coenzyme A biosynthesis: an antimicrobial drug target. Fems Microbiology Reviews. 2008; 32: 56-106.
    • (2008) Fems Microbiology Reviews , vol.32 , pp. 56-106
    • Spry, C.1    Kirk, K.2    Saliba, K.J.3
  • 3
    • 65649151404 scopus 로고    scopus 로고
    • NAD (P) biosynthesis enzymes as potential targets for selective drug design
    • Magni G, Di Stefano M, Orsomando G., et al. NAD (P) biosynthesis enzymes as potential targets for selective drug design. Current Medicinal Chemistry. 2009; 16: 1372-90.
    • (2009) Current Medicinal Chemistry. , vol.16 , pp. 1372-1390
    • Magni, G.1    di Stefano, M.2    Orsomando, G.3
  • 4
    • 0346850972 scopus 로고    scopus 로고
    • Structural biology of enzymes of the thi ami n bi osynthesi s pathway
    • Settembre E, Begley T.P., and Ealick S.E. Structural biology of enzymes of the thi ami n bi osynthesi s pathway. Curr Opi n Struct Biol. 2003; 13: 739-47.
    • (2003) Curr Opi N Struct Biol. , vol.13 , pp. 739-747
    • Settembre, E.1    Begley, T.P.2    Ealick, S.E.3
  • 7
    • 72149097595 scopus 로고    scopus 로고
    • Vitamin B metabolism in Plasmodium falciparum as a source of drug targets
    • Muller I.B, Hyde J.E., and Wrenger C. Vitamin B metabolism in Plasmodium falciparum as a source of drug targets. Trends in Parasitology. 2010; 26: 35-43.
    • (2010) Trends in Parasitology. , vol.26 , pp. 35-43
    • Muller, I.B.1    Hyde, J.E.2    Wrenger, C.3
  • 8
    • 31444454148 scopus 로고    scopus 로고
    • Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase
    • McCourt J.A, Pang S.S., King-Scott J., et al. Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase. Proc Natl Acad Sci U S A. 2006; 103: 569-73.
    • (2006) Proc Natl Acad Sci U S A. , vol.103 , pp. 569-573
    • McCourt, J.A.1    Pang, S.S.2    King-Scott, J.3
  • 9
    • 46649085229 scopus 로고    scopus 로고
    • Inhibitors of Bacillus anthracis acetohydroxyacid synthase
    • Kalme S, Pham C.N., Gedi V., et al. Inhibitors of Bacillus anthracis acetohydroxyacid synthase. Enzyme and Microbial Technology. 2008; 43: 270-275.
    • (2008) Enzyme and Microbial Technology , vol.43 , pp. 270-275
    • Kalme, S.1    Pham, C.N.2    Gedi, V.3
  • 10
    • 24044548711 scopus 로고    scopus 로고
    • Characterization of acetohydroxyacid synthase from Mycobacterium tuberculosis and the identification of its new inhibitor from the screening of a chemical library
    • Choi K.J, Yu Y.G., Hahn H.G., et al. Characterization of acetohydroxyacid synthase from Mycobacterium tuberculosis and the identification of its new inhibitor from the screening of a chemical library. FEBS Lett. 2005; 579: 4903-10.
    • (2005) FEBS Lett. , vol.579 , pp. 4903-4910
    • Choi, K.J.1    Yu, Y.G.2    Hahn, H.G.3
  • 11
    • 0033623202 scopus 로고    scopus 로고
    • Action of the thiamine antagonist bacimethrin on thiamine biosynthesis
    • Zilles J.L, Croal L.R., and Downs D.M. Action of the thiamine antagonist bacimethrin on thiamine biosynthesis. J Bacteriol. 2000; 182: 5606-10.
    • (2000) J Bacteriol. , vol.182 , pp. 5606-5610
    • Zilles, J.L.1    Croal, L.R.2    Downs, D.M.3
  • 12
    • 0035801805 scopus 로고    scopus 로고
    • The mechanism of action of bacimethrin, a naturally occurring thiamin antimetabolite
    • Reddick J.J, Saha S., Lee J., et al. The mechanism of action of bacimethrin, a naturally occurring thiamin antimetabolite. Bioorg Med Chem Lett. 2001; 11: 2245-8.
    • (2001) Bioorg Med Chem Lett. , vol.11 , pp. 2245-2248
    • Reddick, J.J.1    Saha, S.2    Lee, J.3
  • 13
    • 44349089744 scopus 로고    scopus 로고
    • The non-mevalonate pathway to isoprenoid biosynthesis: A potenti al source of new drug targets
    • Hirsch A. K. H and Diederich F. The non-mevalonate pathway to isoprenoid biosynthesis: A potenti al source of new drug targets. Chimia. 2008; 62: 226-230.
    • (2008) Chimia. , vol.62 , pp. 226-230
    • Hirsch, A.K.H.1    Diederich, F.2
  • 14
    • 3042826869 scopus 로고    scopus 로고
    • Inhibition of thiamin diphosphate dependent enzymes by 3-deazathiamin diphosphate
    • Mann S, Melero CP, Hawksley D., et al. Inhibition of thiamin diphosphate dependent enzymes by 3-deazathiamin diphosphate. Organic & Biomolecular Chemistry. 2004; 2: 1732-41.
    • (2004) Organic & Biomolecular Chemistry , vol.2 , pp. 1732-1741
    • Mann, S.1    Melero, C.P.2    Hawksley, D.3
  • 15
    • 33750731272 scopus 로고    scopus 로고
    • Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex
    • Nemeria N.S, Korotchkina L.G., Chakraborty S., et al. Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex. Bioorg Chem. 2006; 34: 362-79.
    • (2006) Bioorg Chem. , vol.34 , pp. 362-379
    • Nemeria, N.S.1    Korotchkina, L.G.2    Chakraborty, S.3
  • 16
    • 34547887970 scopus 로고    scopus 로고
    • Theoretical calculation of the binding free energies for pyruvate dehydrogenase E1 binding with ligands
    • Xiong Y, Li Y., He H., et al. Theoretical calculation of the binding free energies for pyruvate dehydrogenase E1 binding with ligands. Bioorg Med Chem Lett. 2007; 17: 5186-90.
    • (2007) Bioorg Med Chem Lett. , vol.17 , pp. 5186-5190
    • Xiong, Y.1    Li, Y.2    He, H.3
  • 17
    • 0035824606 scopus 로고    scopus 로고
    • Inhibition of the Escherichia coli pyruvate dehydrogenase complex E1 subunit and its tyrosine 177 variants by thiamin 2-thiazolone and thiamin 2-thiothiazolone diphosphates. Evidence for reversible tight-binding inhibition
    • Nemeria N, Yan Y., Zhang Z., et al. Inhibition of the Escherichia coli pyruvate dehydrogenase complex E1 subunit and its tyrosine 177 variants by thiamin 2-thiazolone and thiamin 2-thiothiazolone diphosphates. Evidence for reversible tight-binding inhibition. J Biol Chem. 2001; 276: 45969-78.
    • (2001) J Biol Chem. , vol.276 , pp. 45969-45978
    • Nemeria, N.1    Yan, Y.2    Zhang, Z.3
  • 18
    • 0344223439 scopus 로고    scopus 로고
    • Oxythiamine and dehydroepiandrosterone induce a G1 phase cycle arrest in Ehrlich's tumor cells through inhibition of the pentose cycle
    • Rais B, Comin B., Puigjaner J., et al. Oxythiamine and dehydroepiandrosterone induce a G1 phase cycle arrest in Ehrlich's tumor cells through inhibition of the pentose cycle. FEBS Lett. 1999; 456: 113-8.
    • (1999) FEBS Lett. , vol.456 , pp. 113-118
    • Rais, B.1    Comin, B.2    Puigjaner, J.3
  • 19
    • 38149006234 scopus 로고    scopus 로고
    • Prodrug thiamine analogs as inhibitors of the enzyme transketolase
    • Le Huerou Y, Gunawardana I., Thomas A.A., et al. Prodrug thiamine analogs as inhibitors of the enzyme transketolase. Bioorg Med Chem Lett. 2008; 18: 505-8.
    • (2008) Bioorg Med Chem Lett. , vol.18 , pp. 505-508
    • le Huerou, Y.1    Gunawardana, I.2    Thomas, A.A.3
  • 20
    • 65549130515 scopus 로고    scopus 로고
    • Thiamin diphosphate in biological chemistry: Analogues of thiamin diphosphate in studies of enzymes and riboswitches
    • Agyei-Owusu K and Leeper F.J. Thiamin diphosphate in biological chemistry: analogues of thiamin diphosphate in studies of enzymes and riboswitches. FEBS J. 2009; 276: 2905-16.
    • (2009) FEBS J. , vol.276 , pp. 2905-2916
    • Agyei-Owusu, K.1    Leeper, F.J.2
  • 21
    • 0029944435 scopus 로고    scopus 로고
    • Leuci ne auxotrophy restricts growth of Mycobacterium bovis BCG in macrophages
    • Bange F.C, Brown A.M., and Jacobs W. R. Jr. Leuci ne auxotrophy restricts growth of Mycobacterium bovis BCG in macrophages. Infect Immun. 1996; 64: 1794-9.
    • (1996) Infect Immun. , vol.64 , pp. 1794-1799
    • Bange, F.C.1    Brown, A.M.2    Jacobs Jr W., R.3
  • 22
    • 0029990029 scopus 로고    scopus 로고
    • Auxotrophic vaccines for tuberculosis
    • Guleria I, Teitelbaum R., McAdam R.A., et al. Auxotrophic vaccines for tuberculosis. Nat Med. 1996; 2: 334-7.
    • (1996) Nat Med. , vol.2 , pp. 334-337
    • Guleria, I.1    Teitelbaum, R.2    McAdam, R.A.3
  • 23
    • 0036718269 scopus 로고    scopus 로고
    • A mutant of Burkholderia pseudomallei, auxotrophic in the branched chain amino acid biosynthetic pathway, is attenuated and protective in a murine model of melioidosis
    • Atkins T, Prior R.G., Mack K., et al. A mutant of Burkholderia pseudomallei, auxotrophic in the branched chain amino acid biosynthetic pathway, is attenuated and protective in a murine model of melioidosis. Infect Immun. 2002; 70: 5290-4.
    • (2002) Infect Immun. , vol.70 , pp. 5290-5294
    • Atkins, T.1    Prior, R.G.2    Mack, K.3
  • 24
    • 0043123259 scopus 로고    scopus 로고
    • Acetohydroxyacid synthase from Mycobacterium avium and its inhibition by sulfonylureas and imidazolinones
    • Zohar Y, Einav M., Chipman D.M., et al. Acetohydroxyacid synthase from Mycobacterium avium and its inhibition by sulfonylureas and imidazolinones. Biochim Biophys Acta. 2003; 1649: 97-105.
    • (2003) Biochim Biophys Acta. , vol.1649 , pp. 97-105
    • Zohar, Y.1    Einav, M.2    Chipman, D.M.3
  • 25
    • 43549126424 scopus 로고    scopus 로고
    • In vitro and ex vivo activity of new derivatives of acetohydroxyacid synthase inhibitors against Mycobacterium tuberculosis and non-tuberculous mycobacteria
    • Sohn H, Lee K.S., Ko Y.K., et al. In vitro and ex vivo activity of new derivatives of acetohydroxyacid synthase inhibitors against Mycobacterium tuberculosis and non-tuberculous mycobacteria. Int J Antimicrob Agents. 2008; 31: 567-71.
    • (2008) Int J Antimicrob Agents. , vol.31 , pp. 567-571
    • Sohn, H.1    Lee, K.S.2    Ko, Y.K.3
  • 26
    • 77949914910 scopus 로고    scopus 로고
    • Evaluation of substituted triazol-1-yl-pyrimidines as inhibitors of Bacillus anthracis acetohydroxyacid synthase
    • Gedi V, Jayaraman K., Kalme S., et al. Evaluation of substituted triazol-1-yl-pyrimidines as inhibitors of Bacillus anthracis acetohydroxyacid synthase. Biochim Biophys Acta. 2010; 1804: 1369-75.
    • (2010) Biochim Biophys Acta. , vol.1804 , pp. 1369-1375
    • Gedi, V.1    Jayaraman, K.2    Kalme, S.3
  • 27
    • 79952472051 scopus 로고    scopus 로고
    • Identification of potential P. falciparum transketolase inhibitors: Pharmacophore design, in silico screening and docking studies
    • Joshi S. Identification of potential P. falciparum transketolase inhibitors: pharmacophore design, in silico screening and docking studies. Journal of Biophysical Chemistry. 2010; 01: 96-104.
    • (2010) Journal of Biophysical Chemistry , vol.1 , pp. 96-104
    • Joshi, S.1
  • 28
    • 4744361651 scopus 로고    scopus 로고
    • Biosynthesis of the thiamin pyrimidine: The reconstitution of a remarkable rearrangement reaction
    • Lawhorn B.G, Mehl R.A., and Begley T.P. Biosynthesis of the thiamin pyrimidine: the reconstitution of a remarkable rearrangement reaction. Organic & Biomolecular Chemistry. 2004; 2: 2538-46.
    • (2004) Organic & Biomolecular Chemistry , vol.2 , pp. 2538-2546
    • Lawhorn, B.G.1    Mehl, R.A.2    Begley, T.P.3
  • 29
    • 0027450492 scopus 로고
    • Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12
    • Vander Horn P.B, Backstrom A.D., Stewart V., et al. Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12. J Bacteriol. 1993; 175: 982-92.
    • (1993) J Bacteriol. , vol.175 , pp. 982-992
    • van der Horn, P.B.1    Backstrom, A.D.2    Stewart, V.3
  • 30
    • 0030696041 scopus 로고    scopus 로고
    • Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol
    • Sprenger G.A, Schorken U., Wiegert T., et al. Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol. Proc Natl Acad Sci U S A. 1997; 94: 12857-62.
    • (1997) Proc Natl Acad Sci U S A. , vol.94 , pp. 12857-12862
    • Sprenger, G.A.1    Schorken, U.2    Wiegert, T.3
  • 31
    • 0032568948 scopus 로고    scopus 로고
    • Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation
    • Taylor S.V, Kelleher N.L., Kinsland C., et al. Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation. J Biol Chem. 1998; 273: 16555-60.
    • (1998) J Biol Chem. , vol.273 , pp. 16555-16560
    • Taylor, S.V.1    Kelleher, N.L.2    Kinsland, C.3
  • 32
    • 0035902526 scopus 로고    scopus 로고
    • Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: Identification of an acyldisulfide- linked protein--protein conjugate that is functionally analogous to the ubiquitin/E1 complex
    • Xi J, Ge Y., Kinsland C., et al. Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide- linked protein--protein conjugate that is functionally analogous to the ubiquitin/E1 complex. Proc Natl Acad Sci U S A. 2001; 98: 8513-8.
    • (2001) Proc Natl Acad Sci U S A. , vol.98 , pp. 8513-8518
    • Xi, J.1    Ge, Y.2    Kinsland, C.3
  • 33
    • 0037468666 scopus 로고    scopus 로고
    • Thiamine biosynthesis in Escherichia coli: Isolation and initial characterisation of the ThiGH complex
    • Leonardi R, Fairhurst S.A., Kriek M., et al. Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex. FEBS Lett. 2003; 539: 95-9.
    • (2003) FEBS Lett. , vol.539 , pp. 95-99
    • Leonardi, R.1    Fairhurst, S.A.2    Kriek, M.3
  • 34
    • 4644357750 scopus 로고    scopus 로고
    • Mutational analysis of ThiH, a member of the radical S-adenosylmethionine (AdoMet) protein superfamily
    • Martinez-Gomez N.C, Robers M., and Downs D.M. Mutational analysis of ThiH, a member of the radical S-adenosylmethionine (AdoMet) protein superfamily. Journal of Biological Chemistry. 2004; 279: 40505-40510.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 40505-40510
    • Martinez-Gomez, N.C.1    Robers, M.2    Downs, D.M.3
  • 35
    • 34547107087 scopus 로고    scopus 로고
    • Thiazole synthase from Escherichia coli: An investigation of the substrates and purified proteins required for activity in vitro
    • Kriek M, Martins F., Leonardi R., et al. Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro. J Biol Chem. 2007; 282: 17413-23.
    • (2007) J Biol Chem. , vol.282 , pp. 17413-17423
    • Kriek, M.1    Martins, F.2    Leonardi, R.3
  • 36
    • 0037452907 scopus 로고    scopus 로고
    • Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis
    • Settembre E.C, Dorrestein P.C., Park J.H., et al. Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis. Biochemistry. 2003; 42: 2971-81.
    • (2003) Biochemistry. , vol.42 , pp. 2971-2981
    • Settembre, E.C.1    Dorrestein, P.C.2    Park, J.H.3
  • 37
    • 67650729745 scopus 로고    scopus 로고
    • The structural and biochemical foundations of thiamin biosynthesis
    • Jurgenson C.T, Begley T.P., and Ealick S.E. The structural and biochemical foundations of thiamin biosynthesis. Annu Rev Biochem. 2009; 78: 569-603.
    • (2009) Annu Rev Biochem. , vol.78 , pp. 569-603
    • Jurgenson, C.T.1    Begley, T.P.2    Ealick, S.E.3
  • 38
    • 2442681699 scopus 로고    scopus 로고
    • Identification of the two missing bacterial genes involved in thiamine salvage: Thiamine pyrophosphokinase and thiamine kinase
    • Melnick J, Lis E., Park J.H., et al. Identification of the two missing bacterial genes involved in thiamine salvage: thiamine pyrophosphokinase and thiamine kinase. J Bacteriol. 2004; 186: 3660-2.
    • (2004) J Bacteriol. , vol.186 , pp. 3660-3662
    • Melnick, J.1    Lis, E.2    Park, J.H.3
  • 39
    • 0032502743 scopus 로고    scopus 로고
    • thiBPQ encodes an ABC transporter required for transport of thiamine and thiamine pyrophosphate in Salmonella typhimurium
    • Webb E, Claas K., and Downs D. thiBPQ encodes an ABC transporter required for transport of thiamine and thiamine pyrophosphate in Salmonella typhimurium. J Biol Chem. 1998; 273: 8946-50.
    • (1998) J Biol Chem. , vol.273 , pp. 8946-8950
    • Webb, E.1    Claas, K.2    Downs, D.3
  • 40
    • 0021110758 scopus 로고
    • Transport of 2-methyl-4-amino-5-hydroxymethylpyrimidine by Salmonella typhimurium
    • Bellion E and Lash T.D. Transport of 2-methyl-4-amino-5-hydroxymethylpyrimidine by Salmonella typhimurium. Biochim Biophys Acta. 1983; 735: 337-40.
    • (1983) Biochim Biophys Acta. , vol.735 , pp. 337-340
    • Bellion, E.1    Lash, T.D.2
  • 41
    • 0021110741 scopus 로고
    • Transport of thiamine and 4-methyl-5-hydroxyethylthiazole by Salmonella typhimurium
    • Bellion E, Lash T.D., and McKellar B.R. Transport of thiamine and 4-methyl-5-hydroxyethylthiazole by Salmonella typhimurium. Biochim Biophys Acta. 1983; 735: 331-6.
    • (1983) Biochim Biophys Acta. , vol.735 , pp. 331-336
    • Bellion, E.1    Lash, T.D.2    McKellar, B.R.3
  • 42
    • 2242446202 scopus 로고    scopus 로고
    • Comparative genomics of thiamin biosynthesis in procaryotes. New genes and regulatory mechanisms
    • Rodionov D.A, Vitreschak A.G., Mironov A.A., et al. Comparative genomics of thiamin biosynthesis in procaryotes. New genes and regulatory mechanisms. J Biol Chem. 2002; 277: 48949-59.
    • (2002) J Biol Chem. , vol.277 , pp. 48949-48959
    • Rodionov, D.A.1    Vitreschak, A.G.2    Mironov, A.A.3
  • 43
    • 4644337995 scopus 로고    scopus 로고
    • The structure and ligand binding properties of the B. subtilis YkoF gene product, a member of a novel family of thiamin/HMP-binding proteins
    • Devedjiev Y, Surendranath Y., Derewenda U., et al. The structure and ligand binding properties of the B. subtilis YkoF gene product, a member of a novel family of thiamin/HMP-binding proteins. J Mol Biol. 2004; 343: 395-406.
    • (2004) J Mol Biol. , vol.343 , pp. 395-406
    • Devedjiev, Y.1    Surendranath, Y.2    Derewenda, U.3
  • 44
    • 38849104227 scopus 로고    scopus 로고
    • Comparative genomics and functional annotation of bacterial transporters
    • Gelfand M.S and Rodionov D.A. Comparative genomics and functional annotation of bacterial transporters. Physics of Life Reviews. 2008; 5: 22-49.
    • (2008) Physics of Life Reviews , vol.5 , pp. 22-49
    • Gelfand, M.S.1    Rodionov, D.A.2
  • 46
    • 0022576963 scopus 로고
    • Differences in susceptibility to quinolones of outer membrane mutants of Salmonella typhimurium and Escherichia coli
    • Hirai K, Aoyama H., Irikura T., et al. Differences in susceptibility to quinolones of outer membrane mutants of Salmonella typhimurium and Escherichia coli. Antimicrob Agents Chemother. 1986; 29: 535-8.
    • (1986) Antimicrob Agents Chemother. , vol.29 , pp. 535-538
    • Hirai, K.1    Aoyama, H.2    Irikura, T.3
  • 47
  • 48
    • 64049101182 scopus 로고    scopus 로고
    • Both thiamine uptake and biosynthesis of thiamine precursors are required for intracellular replication of Listeria monocytogenes
    • Schauer K, Stolz J., Scherer S., et al. Both thiamine uptake and biosynthesis of thiamine precursors are required for intracellular replication of Listeria monocytogenes. J Bacteriol. 2009; 191: 2218-27.
    • (2009) J Bacteriol. , vol.191 , pp. 2218-2227
    • Schauer, K.1    Stolz, J.2    Scherer, S.3
  • 49
    • 0029938615 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoids (carotenoids, sterols, prenyl side-chains of chlorophylls and plastoquinone) via a novel pyruvate/ glyceraldehyde 3-phosphate non-mevalonate pathway in the green alga Scenedesmus obliquus
    • Schwender J, Seemann M., Lichtenthaler H.K., et al. Biosynthesis of isoprenoids (carotenoids, sterols, prenyl side-chains of chlorophylls and plastoquinone) via a novel pyruvate/ glyceraldehyde 3-phosphate non-mevalonate pathway in the green alga Scenedesmus obliquus. Biochem J. 1996; 316 (Pt 1): 73-80.
    • (1996) Biochem J. , vol.316 , Issue.PART 1 , pp. 73-80
    • Schwender, J.1    Seemann, M.2    Lichtenthaler, H.K.3
  • 50
    • 0029846427 scopus 로고    scopus 로고
    • The biogenetic anatomy of vitamin B6. A 13C NMR investigation of the biosynthesis of pyridoxol in Escherichia coli
    • Hill R.E, Himmeldirk K., Kennedy I.A., et al. The biogenetic anatomy of vitamin B6. A 13C NMR investigation of the biosynthesis of pyridoxol in Escherichia coli. J Biol Chem. 1996; 271: 30426-35.
    • (1996) J Biol Chem. , vol.271 , pp. 30426-30435
    • Hill, R.E.1    Himmeldirk, K.2    Kennedy, I.A.3
  • 51
    • 0034700150 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis: The evolution of two ancient and distinct pathways across genomes
    • Lange B.M, Rujan T., Martin W., et al. Isoprenoid biosynthesis: the evolution of two ancient and distinct pathways across genomes. Proc Natl Acad Sci U S A. 2000; 97: 13172-7.
    • (2000) Proc Natl Acad Sci U S A. , vol.97 , pp. 13172-13177
    • Lange, B.M.1    Rujan, T.2    Martin, W.3
  • 52
    • 34047252866 scopus 로고    scopus 로고
    • Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis
    • Xiang S, Usunow G., Lange G., et al. Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis. J Biol Chem. 2007; 282: 2676-82.
    • (2007) J Biol Chem. , vol.282 , pp. 2676-2682
    • Xiang, S.1    Usunow, G.2    Lange, G.3
  • 53
    • 0034666627 scopus 로고    scopus 로고
    • Tools for discovery of inhibitors of the 1-deoxy-D-xylulose 5-phosphate (DXP) synthase and DXP reductoisomerase: An approach with enzymes from the pathogenic bacterium Pseudomonas aeruginosa
    • Altincicek B, Hintz M., Sanderbrand S., et al. Tools for discovery of inhibitors of the 1-deoxy-D-xylulose 5-phosphate (DXP) synthase and DXP reductoisomerase: an approach with enzymes from the pathogenic bacterium Pseudomonas aeruginosa. FEMS Microbiol Lett. 2000; 190: 329-33.
    • (2000) FEMS Microbiol Lett. , vol.190 , pp. 329-333
    • Altincicek, B.1    Hintz, M.2    Sanderbrand, S.3
  • 54
    • 0034472991 scopus 로고    scopus 로고
    • Properties and inhibition of the first two enzymes of the non-mevalonate pathway of isoprenoid biosynthesis
    • Mueller C, Schwender J., Zeidler J., et al. Properties and inhibition of the first two enzymes of the non-mevalonate pathway of isoprenoid biosynthesis. Biochem Soc Trans. 2000; 28: 792-3.
    • (2000) Biochem Soc Trans. , vol.28 , pp. 792-793
    • Mueller, C.1    Schwender, J.2    Zeidler, J.3
  • 55
    • 0034471574 scopus 로고    scopus 로고
    • The non-mevalonate isoprenoid biosynthesis of plants as a test system for drugs against malaria and pathogenic bacteria
    • Zeidler J, Schwender J., Mueller C., et al. The non-mevalonate isoprenoid biosynthesis of plants as a test system for drugs against malaria and pathogenic bacteria. Biochem Soc Trans. 2000; 28: 796-8.
    • (2000) Biochem Soc Trans. , vol.28 , pp. 796-798
    • Zeidler, J.1    Schwender, J.2    Mueller, C.3
  • 56
    • 3042782938 scopus 로고    scopus 로고
    • The MEP pathway: A new target for the development of herbicides, antibiotics and antimalarial drugs
    • Rodriguez-Concepcion M. The MEP pathway: a new target for the development of herbicides, antibiotics and antimalarial drugs. Curr Pharm Des. 2004; 10: 2391-400.
    • (2004) Curr Pharm Des. , vol.10 , pp. 2391-2400
    • Rodriguez-Concepcion, M.1
  • 57
    • 52049084364 scopus 로고    scopus 로고
    • Structure-activity relationships of compounds targeting mycobacterium tuberculosis 1-deoxy-D-xylulose 5-phosphate synthase
    • Mao J, Eoh H., He R., et al. Structure-activity relationships of compounds targeting mycobacterium tuberculosis 1-deoxy-D-xylulose 5-phosphate synthase. Bioorg Med Chem Lett. 2008; 18: 5320-3.
    • (2008) Bioorg Med Chem Lett. , vol.18 , pp. 5320-5323
    • Mao, J.1    Eoh, H.2    He, R.3
  • 58
    • 0033580644 scopus 로고    scopus 로고
    • Crystal structure of thiamin phosphate synthase from Bacillus subtilis at 1.25 A resolution
    • Chiu H.J, Reddick J.J., Begley T.P., et al. Crystal structure of thiamin phosphate synthase from Bacillus subtilis at 1.25 A resolution. Biochemistry. 1999; 38: 6460-70.
    • (1999) Biochemistry , vol.38 , pp. 6460-6470
    • Chiu, H.J.1    Reddick, J.J.2    Begley, T.P.3
  • 59
    • 38649093630 scopus 로고    scopus 로고
    • Sensitive genome- wide screen for low secondary enzymatic activities: The YjbQ family shows thiamin phosphate synthase activity
    • Morett E, Saab-Rincon G., Olvera L., et al. Sensitive genome- wide screen for low secondary enzymatic activities: the YjbQ family shows thiamin phosphate synthase activity. J Mol Biol. 2008; 376: 839-53.
    • (2008) J Mol Biol. , vol.376 , pp. 839-853
    • Morett, E.1    Saab-Rincon, G.2    Olvera, L.3
  • 60
    • 0035964270 scopus 로고    scopus 로고
    • Mechanistic studies on thiamin phosphate synthase: Evidence for a dissociative mechanism
    • Reddick J.J, Nicewonger R., and Begley T.P. Mechanistic studies on thiamin phosphate synthase: evidence for a dissociative mechanism. Biochemistry. 2001; 40: 10095-102.
    • (2001) Biochemistry. , vol.40 , pp. 10095-10102
    • Reddick, J.J.1    Nicewonger, R.2    Begley, T.P.3
  • 61
    • 0142126717 scopus 로고    scopus 로고
    • Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1)
    • Park J.H, Dorrestein P.C., Zhai H., et al. Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1). Biochemistry. 2003; 42: 12430-8.
    • (2003) Biochemistry. , vol.42 , pp. 12430-12438
    • Park, J.H.1    Dorrestein, P.C.2    Zhai, H.3
  • 62
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti C.M, Boyd D.H., and Rubin E.J. Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol. 2003; 48: 77-84.
    • (2003) Mol Microbiol. , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 64
    • 0346687595 scopus 로고    scopus 로고
    • The riboswitch control of bacterial metabolism
    • Nudler E and Mironov A.S. The riboswitch control of bacterial metabolism. Trends Biochem Sci. 2004; 29: 11-7.
    • (2004) Trends Biochem Sci. , vol.29 , pp. 11-17
    • Nudler, E.1    Mironov, A.S.2
  • 65
    • 2942549198 scopus 로고    scopus 로고
    • Ri boswitches exert geneti c control through metabolite-induced conformational change
    • Soukup J. K and Soukup G. A. Ri boswitches exert geneti c control through metabolite-induced conformational change. Curr Opin Struct Biol. 2004; 14: 344-9.
    • (2004) Curr Opin Struct Biol. , vol.14 , pp. 344-349
    • Soukup, J.K.1    Soukup, G.A.2
  • 67
    • 70350771280 scopus 로고    scopus 로고
    • A trans-acting riboswitch controls expression of the virulence regulator PrfA in Listeria monocytogenes
    • Loh E, Dussurget O., Gripenland J., et al. A trans-acting riboswitch controls expression of the virulence regulator PrfA in Listeria monocytogenes. Cell. 2009; 139: 770-9.
    • (2009) Cell. , vol.139 , pp. 770-779
    • Loh, E.1    Dussurget, O.2    Gripenland, J.3
  • 68
    • 41349118107 scopus 로고    scopus 로고
    • Complex riboswitches
    • Breaker R.R. Complex riboswitches. Science. 2008; 319: 1795-7.
    • (2008) Science. , vol.319 , pp. 1795-1797
    • Breaker, R.R.1
  • 69
    • 67650713931 scopus 로고    scopus 로고
    • The structural and functional diversity of metabolite-binding riboswitches
    • Roth A and Breaker R.R. The structural and functional diversity of metabolite-binding riboswitches. Annu Rev Biochem. 2009; 78: 305-34.
    • (2009) Annu Rev Biochem. , vol.78 , pp. 305-334
    • Roth, A.1    Breaker, R.R.2
  • 70
    • 0346366823 scopus 로고    scopus 로고
    • Thiamine- regulated gene expression of Aspergillus oryzae thiA requires splicing of the intron containing a riboswitch-like domain in the 5'-UTR
    • Kubodera T, Watanabe M., Yoshiuchi K., et al. Thiamine- regulated gene expression of Aspergillus oryzae thiA requires splicing of the intron containing a riboswitch-like domain in the 5'-UTR. FEBS Lett. 2003; 555: 516-20.
    • (2003) FEBS Lett. , vol.555 , pp. 516-520
    • Kubodera, T.1    Watanabe, M.2    Yoshiuchi, K.3
  • 71
    • 0035859828 scopus 로고    scopus 로고
    • A conserved RNA structure (thi box) is involved in regulation of thiamin biosynthetic gene expression in bacteria
    • Miranda-Rios J, Navarro M., and Soberon M. A conserved RNA structure (thi box) is involved in regulation of thiamin biosynthetic gene expression in bacteria. Proc Natl Acad Sci U S A. 2001; 98: 9736-41.
    • (2001) Proc Natl Acad Sci U S A. , vol.98 , pp. 9736-9741
    • Miranda-Rios, J.1    Navarro, M.2    Soberon, M.3
  • 72
    • 0038136962 scopus 로고    scopus 로고
    • Metabolite-binding RNA domains are present in the genes of eukaryotes
    • Sudarsan N, Barrick J.E., and Breaker R.R. Metabolite-binding RNA domains are present in the genes of eukaryotes. RNA. 2003; 9: 644-7.
    • (2003) RNA , vol.9 , pp. 644-647
    • Sudarsan, N.1    Barrick, J.E.2    Breaker, R.R.3
  • 73
    • 34447508064 scopus 로고    scopus 로고
    • At the crossroad of thiamine degradation and biosynthesis
    • Bettendorff L. At the crossroad of thiamine degradation and biosynthesis. Nat Chem Biol. 2007; 3: 454-5.
    • (2007) Nat Chem Biol. , vol.3 , pp. 454-455
    • Bettendorff, L.1
  • 74
    • 38049169167 scopus 로고    scopus 로고
    • Thiamine biosynthesis in algae is regulated by riboswitches
    • Croft M.T, Moulin M., Webb M.E., et al. Thiamine biosynthesis in algae is regulated by riboswitches. Proc Natl Acad Sci U S A. 2007; 104: 20770-5.
    • (2007) Proc Natl Acad Sci U S A. , vol.104 , pp. 20770-20775
    • Croft, M.T.1    Moulin, M.2    Webb, M.E.3
  • 75
    • 38549119502 scopus 로고    scopus 로고
    • Abundance M.S and functional diversity of riboswitches in microbial communities
    • Kazanov M.D, Vitreschak A.G., and Gelfand MS. Abundance M.S and functional diversity of riboswitches in microbial communities. BMC Genomics. 2007; 8: 347.
    • (2007) BMC Genomics. , vol.8 , pp. 347
    • Kazanov, M.D.1    Vitreschak, A.G.2    Gelfand, M.S.3
  • 76
    • 33745635350 scopus 로고    scopus 로고
    • Structural basis for gene regulation by a thiamine pyrophosphate-sensing riboswitch
    • Serganov A, Polonskaia A., Phan A.T., et al. Structural basis for gene regulation by a thiamine pyrophosphate-sensing riboswitch. Nature. 2006; 441: 1167-71.
    • (2006) Nature. , vol.441 , pp. 1167-1171
    • Serganov, A.1    Polonskaia, A.2    Phan, A.T.3
  • 77
    • 33744469562 scopus 로고    scopus 로고
    • Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand
    • Thore S, Leibundgut M., and Ban N. Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand. Science. 2006; 312: 1208-11.
    • (2006) Science. , vol.312 , pp. 1208-1211
    • Thore, S.1    Leibundgut, M.2    Ban, N.3
  • 78
    • 33845700514 scopus 로고    scopus 로고
    • Riboswitches as antibacterial drug targets
    • Blount K.F and Breaker R.R. Riboswitches as antibacterial drug targets. Nat Biotechnol. 2006; 24: 1558-64.
    • (2006) Nat Biotechnol. , vol.24 , pp. 1558-1564
    • Blount, K.F.1    Breaker, R.R.2
  • 79
    • 33745685059 scopus 로고    scopus 로고
    • Flipping riboswitches
    • Nudler E. Flipping riboswitches. Cell. 2006; 126: 19-22.
    • (2006) Cell. , vol.126 , pp. 19-22
    • Nudler, E.1
  • 80
    • 0033120034 scopus 로고    scopus 로고
    • The mechanism of intrinsic transcription termination
    • Gusarov I and Nudler E. The mechanism of intrinsic transcription termination. Mol Cell. 1999; 3: 495-504.
    • (1999) Mol Cell. , vol.3 , pp. 495-504
    • Gusarov, I.1    Nudler, E.2
  • 81
    • 0033597435 scopus 로고    scopus 로고
    • Mechanism of intrinsic transcription termination and antitermination
    • Yarnell W.S and Roberts J.W. Mechanism of intrinsic transcription termination and antitermination. Science. 1999; 284: 611-5.
    • (1999) Science. , vol.284 , pp. 611-615
    • Yarnell, W.S.1    Roberts, J.W.2
  • 82
    • 43149103943 scopus 로고    scopus 로고
    • Targeting RNA with small molecules
    • Thomas J.R and Hergenrother P.J. Targeting RNA with small molecules. Chem Rev. 2008; 108: 1171-224.
    • (2008) Chem Rev. , vol.108 , pp. 1171-1224
    • Thomas, J.R.1    Hergenrother, P.J.2
  • 83
    • 33644504461 scopus 로고    scopus 로고
    • Antibacterial drug discovery-- then, now and the genomics future
    • Monaghan R.L and Barrett J.F. Antibacterial drug discovery-- then, now and the genomics future. Biochem Pharmacol. 2006; 71: 901-9.
    • (2006) Biochem Pharmacol. , vol.71 , pp. 901-909
    • Monaghan, R.L.1    Barrett, J.F.2
  • 84
    • 28844492215 scopus 로고    scopus 로고
    • Thiamine pyrophosphate riboswitches are targets for the antimicrobial compound pyrithiamine
    • Sudarsan N, Cohen-Chalamish S., Nakamura S., et al. Thiamine pyrophosphate riboswitches are targets for the antimicrobial compound pyrithiamine. Chem Biol. 2005; 12: 1325-35.
    • (2005) Chem Biol. , vol.12 , pp. 1325-1335
    • Sudarsan, N.1    Cohen-Chalamish, S.2    Nakamura, S.3
  • 85
    • 77954079519 scopus 로고    scopus 로고
    • Novel riboswitch ligand analogs as selective inhibitors of guanine-related metabolic pathways
    • Mulhbacher J, Brouillette E., Allard M., et al. Novel riboswitch ligand analogs as selective inhibitors of guanine-related metabolic pathways. PLoS Pathog. 2010; 6: e1000865.
    • (2010) PLoS Pathog. , vol.6
    • Mulhbacher, J.1    Brouillette, E.2    Allard, M.3
  • 86
    • 73449116019 scopus 로고    scopus 로고
    • Design and antimicrobial action of purine analogues that bind Guanine riboswitches
    • Kim J.N, Blount K.F., Puskarz I., et al. Design and antimicrobial action of purine analogues that bind Guanine riboswitches. ACS Chem Biol. 2009; 4: 915-27.
    • (2009) ACS Chem Biol. , vol.4 , pp. 915-927
    • Kim, J.N.1    Blount, K.F.2    Puskarz, I.3
  • 87
    • 33845745224 scopus 로고    scopus 로고
    • 'Turning on' riboswitches to their antibacterial potential
    • Lea C.R and Piccirilli J.A. 'Turning on' riboswitches to their antibacterial potential. Nat Chem Biol. 2007; 3: 16-7.
    • (2007) Nat Chem Biol. , vol.3 , pp. 16-17
    • Lea, C.R.1    Piccirilli, J.A.2
  • 88
    • 60349085695 scopus 로고    scopus 로고
    • Riboswitches: Ancient and promising genetic regulators
    • Blouin S, Mulhbacher J., Penedo J.C., et al. Riboswitches: ancient and promising genetic regulators. Chembiochem. 2009; 10: 400-16.
    • (2009) Chembiochem. , vol.10 , pp. 400-416
    • Blouin, S.1    Mulhbacher, J.2    Penedo, J.C.3
  • 89
    • 70349199881 scopus 로고    scopus 로고
    • Riboswitches: From ancient gene-control systems to modern drug targets
    • Breaker R.R. Riboswitches: from ancient gene-control systems to modern drug targets. Future Microbiol. 2009; 4: 771-3.
    • (2009) Future Microbiol. , vol.4 , pp. 771-773
    • Breaker, R.R.1
  • 90
    • 22644447865 scopus 로고    scopus 로고
    • Variant tricarboxylic acid cycle in Mycobacterium tuberculosis: Identification of alpha- ketoglutarate decarboxylase
    • Tian J, Bryk R., Itoh M., et al. Variant tricarboxylic acid cycle in Mycobacterium tuberculosis: identification of alpha- ketoglutarate decarboxylase. Proc Natl Acad Sci U S A. 2005; 102: 10670-5.
    • (2005) Proc Natl Acad Sci U S A. , vol.102 , pp. 10670-10675
    • Tian, J.1    Bryk, R.2    Itoh, M.3


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