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Volumn 10, Issue 18, 2010, Pages 1858-1871

Isoprenoid metabolism as a therapeutic target in gram-negative pathogens

Author keywords

Bisphosphonate; Escherichia coli; Farnesyl diphosphate; Farnesyl pyrophosphate; Geranylgeranyl diphosphate synthase; Gram negative; Isoprene; MEP pathway; Mevalonate pathway; Terpene

Indexed keywords

ANTIBIOTIC AGENT; FARNESYL DIPHOSPHATE; FOSMIDOMYCIN; ISOPRENE; ISOPRENOID; MENAQUINONE; PEPTIDOGLYCAN; PLASTOQUINONE; PROTEIN FARNESYLTRANSFERASE; QUINONE DERIVATIVE; RHODOQUINONE; SYNTHETASE; TRANSFERASE; UBIQUINONE; UNCLASSIFIED DRUG;

EID: 78649969466     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802610793176602     Document Type: Article
Times cited : (27)

References (117)
  • 1
    • 0031984684 scopus 로고    scopus 로고
    • Diarrheagenic Escherichia coli
    • Nataro, J. P. and Kaper, J. B. Diarrheagenic Escherichia coli. Clin. Microbiol. Rev., 1998, 11, 142-201.
    • (1998) Clin. Microbiol. Rev , vol.11 , pp. 142-201
    • Nataro, J.P.1    Kaper, J.B.2
  • 2
    • 70349328033 scopus 로고    scopus 로고
    • Salmonellosis outbreaks in the United States due to fresh produce: Sources and potential intervention measures
    • Hanning, I. B.; Nutt, J. D.; Ricke, S. C. Salmonellosis outbreaks in the United States due to fresh produce: sources and potential intervention measures. Foodborne Pathog. Dis., 2009, 6, 635-648.
    • (2009) Foodborne Pathog. Dis , vol.6 , pp. 635-648
    • Hanning, I.B.1    Nutt, J.D.2    Ricke, S.C.3
  • 4
    • 19344366789 scopus 로고    scopus 로고
    • Shigellosis
    • Niyogi, S. K. Shigellosis. J. Microbiol., 2005, 43, 133-143.
    • (2005) J. Microbiol , vol.43 , pp. 133-143
    • Niyogi, S.K.1
  • 5
    • 33845314004 scopus 로고    scopus 로고
    • Phytoplankton and cloudiness in the Southern Ocean
    • Meskhidze, N.; Nenes, A. Phytoplankton and cloudiness in the Southern Ocean. Science, 2006, 314, 1419-1423.
    • (2006) Science , vol.314 , pp. 1419-1423
    • Meskhidze, N.1    Nenes, A.2
  • 7
    • 67651096109 scopus 로고    scopus 로고
    • The intermediate enzymes of isoprenoid metabolism as anticancer targets
    • Wiemer, A. J.; Hohl, R. J.; Wiemer, D. F. The intermediate enzymes of isoprenoid metabolism as anticancer targets. Anticancer Agents Med. Chem., 2009, 9, 526-542.
    • (2009) Anticancer Agents Med. Chem , vol.9 , pp. 526-542
    • Wiemer, A.J.1    Hohl, R.J.2    Wiemer, D.F.3
  • 8
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J. L.; Brown, M. S. Regulation of the mevalonate pathway. Nature, 1990, 343, 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 10
    • 0000007179 scopus 로고
    • Mevalonic kinase: Purification and properties
    • Tchen, T. T. Mevalonic kinase: purification and properties. J. Biol. Chem., 1958, 233, 1100-1103.
    • (1958) J. Biol. Chem , vol.233 , pp. 1100-1103
    • Tchen, T.T.1
  • 11
    • 0032964743 scopus 로고    scopus 로고
    • Characterization of phosphomevalonate kinase: Chromosomal localization, regulation, and subcellular targeting
    • Olivier, L. M.; Chambliss, K. L.; Gibson, K. M.; Krisans, S. K. Characterization of phosphomevalonate kinase: chromosomal localization, regulation, and subcellular targeting. J. Lipid Res., 1999, 40, 672-679.
    • (1999) J. Lipid Res , vol.40 , pp. 672-679
    • Olivier, L.M.1    Chambliss, K.L.2    Gibson, K.M.3    Krisans, S.K.4
  • 12
    • 0030016345 scopus 로고    scopus 로고
    • Molecular cloning of human phosphomevalonate kinase and identification of a consensus peroxisomal targeting sequence
    • Chambliss, K. L.; Slaughter, C. A.; Schreiner, R.; Hoffmann, G. F.; Gibson, K. M. Molecular cloning of human phosphomevalonate kinase and identification of a consensus peroxisomal targeting sequence. J. Biol. Chem., 1996, 271, 17330-17334.
    • (1996) J. Biol. Chem , vol.271 , pp. 17330-17334
    • Chambliss, K.L.1    Slaughter, C.A.2    Schreiner, R.3    Hoffmann, G.F.4    Gibson, K.M.5
  • 13
    • 0024222843 scopus 로고
    • Physiological aspects and mechanism of action of mevalonate 5-diphosphate decarboxylase
    • Jabalquinto, A. M.; Alvear, M.; Cardemil, E. Physiological aspects and mechanism of action of mevalonate 5-diphosphate decarboxylase. Comp. Biochem. Physiol. B, 1988, 90, 671-677.
    • (1988) Comp. Biochem. Physiol. B , vol.90 , pp. 671-677
    • Jabalquinto, A.M.1    Alvear, M.2    Cardemil, E.3
  • 14
    • 0027368126 scopus 로고
    • Isoprenoid biosynthesis in bacteria: A novel pathway for the early steps leading to isopentenyl diphosphate
    • Rohmer, M.; Knani, M.; Simonin, P.; Sutter, B.; Sahm, H. Isoprenoid biosynthesis in bacteria: a novel pathway for the early steps leading to isopentenyl diphosphate. Biochem. J., 1993, 295 (Pt 2), 517-524.
    • (1993) Biochem. J , vol.295 , Issue.Pt 2 , pp. 517-524
    • Rohmer, M.1    Knani, M.2    Simonin, P.3    Sutter, B.4    Sahm, H.5
  • 15
    • 0000725115 scopus 로고    scopus 로고
    • Distribution of mevalonate and glyceraldehyde 3-phosphate/pyruvate routes for isoprenoid biosynthesis in some gram-negative bacteria and mycobacteria
    • Putra, S. R.; Disch, A.; Bravo, J. M.; Rohmer, M. Distribution of mevalonate and glyceraldehyde 3-phosphate/pyruvate routes for isoprenoid biosynthesis in some gram-negative bacteria and mycobacteria. FEMS Microbiol. Lett., 1998, 164, 169-175.
    • (1998) FEMS Microbiol. Lett , vol.164 , pp. 169-175
    • Putra, S.R.1    Disch, A.2    Bravo, J.M.3    Rohmer, M.4
  • 16
    • 34547609909 scopus 로고    scopus 로고
    • The non-mevalonate pathway of isoprenoid precursor biosynthesis
    • Hunter, W. N. The non-mevalonate pathway of isoprenoid precursor biosynthesis. J. Biol. Chem., 2007, 282, 21573-21577.
    • (2007) J. Biol. Chem , vol.282 , pp. 21573-21577
    • Hunter, W.N.1
  • 18
    • 71049170515 scopus 로고    scopus 로고
    • Coordination chemistry based approach to lipophilic inhibitors of 1-Deoxyd- xylulose-5-phosphate Reductoisomerase
    • Deng, L.; Sundriyal, S.; Rubio, V.; Shi, Z.-z.; Song, Y. Coordination chemistry based approach to lipophilic inhibitors of 1-Deoxyd- xylulose-5-phosphate Reductoisomerase. J. Med. Chem., 2009, 52, 6539-6542.
    • (2009) J. Med. Chem , vol.52 , pp. 6539-6542
    • Deng, L.1    Sundriyal, S.2    Rubio, V.3    Shi, Z.-z.4    Song, Y.5
  • 19
    • 28844484972 scopus 로고    scopus 로고
    • 1-Deoxy-D-xylulose 5-phosphate reductoisomerase (IspC) from Mycobacterium tuberculosis: Towards understanding mycobacterial resistance to fosmidomycin
    • Dhiman, R. K.; Schaeffer, M. L.; Bailey, A. M.; Testa, C. A.; Scherman, H.; Crick, D. C. 1-Deoxy-D-xylulose 5-phosphate reductoisomerase (IspC) from Mycobacterium tuberculosis: towards understanding mycobacterial resistance to fosmidomycin. J. Bacteriol., 2005, 187, 8395-8402.
    • (2005) J. Bacteriol , vol.187 , pp. 8395-8402
    • Dhiman, R.K.1    Schaeffer, M.L.2    Bailey, A.M.3    Testa, C.A.4    Scherman, H.5    Crick, D.C.6
  • 20
    • 2842613801 scopus 로고    scopus 로고
    • Fosmidomycin resistance in adenylate cyclase deficient (cya) mutants of Escherichia coli
    • Sakamoto, Y.; Furukawa, S.; Ogihara, H.; Yamasaki, M. Fosmidomycin resistance in adenylate cyclase deficient (cya) mutants of Escherichia coli. Biosci. Biotechnol. Biochem., 2003, 67, 2030-2033.
    • (2003) Biosci. Biotechnol. Biochem , vol.67 , pp. 2030-2033
    • Sakamoto, Y.1    Furukawa, S.2    Ogihara, H.3    Yamasaki, M.4
  • 21
    • 33644851756 scopus 로고    scopus 로고
    • Cloning and expression of IspDF from Mesorhizobium loti. Characterization of a bifunctional protein that catalyzes non-consecutive steps in the methylerythritol phosphate pathway
    • Testa, C. A.; Lherbet, C.; Pojer, F.; Noel, J. P.; Poulter, C. D. Cloning and expression of IspDF from Mesorhizobium loti. Characterization of a bifunctional protein that catalyzes non-consecutive steps in the methylerythritol phosphate pathway. Biochim Biophys Acta - Proteins Proteomics, 2006, 1764, 85-96.
    • (2006) Biochim Biophys Acta - Proteins Proteomics , vol.1764 , pp. 85-96
    • Testa, C.A.1    Lherbet, C.2    Pojer, F.3    Noel, J.P.4    Poulter, C.D.5
  • 22
    • 32444443111 scopus 로고    scopus 로고
    • Lethal mutations in the isoprenoid pathway of Salmonella enterica
    • Cornish, R. M.; Roth, J. R.; Poulter, C. D. Lethal mutations in the isoprenoid pathway of Salmonella enterica. J. Bacteriol., 2006, 188, 1444-1450.
    • (2006) J. Bacteriol , vol.188 , pp. 1444-1450
    • Cornish, R.M.1    Roth, J.R.2    Poulter, C.D.3
  • 23
    • 67651086146 scopus 로고
    • Intermediates in the conversion of mevalonic acid to squalene by a rat liver enzyme system
    • Witting, L. A. and Porter, J. W. Intermediates in the conversion of mevalonic acid to squalene by a rat liver enzyme system. J. Biol. Chem., 1959, 234, 2841-2846.
    • (1959) J. Biol. Chem , vol.234 , pp. 2841-2846
    • Witting, L.A.1    Porter, J.W.2
  • 24
    • 38949211472 scopus 로고    scopus 로고
    • Small molecules for the activation of human gammadelta T cell responses against infection
    • Kabelitz, D. Small molecules for the activation of human gammadelta T cell responses against infection. Recent Pat. Antiinfect. Drug Discov., 2008, 3, 1-9.
    • (2008) Recent Pat. Antiinfect. Drug Discov , vol.3 , pp. 1-9
    • Kabelitz, D.1
  • 25
    • 33845473042 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis as a drug target: Bisphosphonate inhibition of Escherichia coli K12 growth and synergistic effects of Fosmidomycin
    • Leon, A.; Liu, L.; Yang, Y.; Hudock, M. P.; Hall, P.; Yin, F.; Studer, D.; Puan, K.-J.; Morita, C. T.; Oldfield, E. Isoprenoid biosynthesis as a drug target: bisphosphonate inhibition of Escherichia coli K12 growth and synergistic effects of Fosmidomycin. J. Med. Chem., 2006, 49, 7331-7341.
    • (2006) J. Med. Chem , vol.49 , pp. 7331-7341
    • Leon, A.1    Liu, L.2    Yang, Y.3    Hudock, M.P.4    Hall, P.5    Yin, F.6    Studer, D.7    Puan, K.-J.8    Morita, C.T.9    Oldfield, E.10
  • 26
    • 58149492519 scopus 로고    scopus 로고
    • Different reaction mechanisms for cis- and trans-prenyltransferases
    • Lu, Y. P.; Liu, H. G.; Liang, P. H. Different reaction mechanisms for cis- and trans-prenyltransferases. Biochem. Biophys. Res. Comm., 2009, 379, 351-355.
    • (2009) Biochem. Biophys. Res. Comm , vol.379 , pp. 351-355
    • Lu, Y.P.1    Liu, H.G.2    Liang, P.H.3
  • 27
    • 0030970352 scopus 로고    scopus 로고
    • Expression of an exogenous isopentenyl diphosphate isomerase gene enhances isoprenoid biosynthesis in Escherichia coli
    • Kajiwara, S.; Fraser, P. D.; Kondo, K.; Misawa, N. Expression of an exogenous isopentenyl diphosphate isomerase gene enhances isoprenoid biosynthesis in Escherichia coli. Biochem. J, 1997, 324 (Pt 2), 421-426.
    • (1997) Biochem. J , vol.324 , Issue.Pt 2 , pp. 421-426
    • Kajiwara, S.1    Fraser, P.D.2    Kondo, K.3    Misawa, N.4
  • 28
    • 0027971410 scopus 로고
    • Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4'- diaponeurosporene of Staphylococcus aureus
    • Wieland, B.; Feil, C.; Gloria-Maercker, E.; Thumm, G.; Lechner, M.; Bravo, J. M.; Poralla, K.; Gotz, F. Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4'- diaponeurosporene of Staphylococcus aureus. J. Bacteriol., 1994, 176, 7719-7726.
    • (1994) J. Bacteriol , vol.176 , pp. 7719-7726
    • Wieland, B.1    Feil, C.2    Gloria-Maercker, E.3    Thumm, G.4    Lechner, M.5    Bravo, J.M.6    Poralla, K.7    Gotz, F.8
  • 29
    • 32544441906 scopus 로고    scopus 로고
    • A soluble form of phosphatase in Saccharomyces cerevisiae capable of converting farnesyl diphosphate into E, E-farnesol
    • Song, L. S. A soluble form of phosphatase in Saccharomyces cerevisiae capable of converting farnesyl diphosphate into E, E-farnesol. Appl. Biochem. Biotechnol., 2006, 128, 149-157.
    • (2006) Appl. Biochem. Biotechnol , vol.128 , pp. 149-157
    • Song, L.S.1
  • 30
    • 0034670571 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of the geometric farnesylated analogues of the a-factor mating peptide of Saccharomyces cerevisiae
    • Xie, H.; Shao, Y.; Becker, J. M.; Naider, F.; Gibbs, R. A. Synthesis and biological evaluation of the geometric farnesylated analogues of the a-factor mating peptide of Saccharomyces cerevisiae. J. Org. Chem., 2000, 65, 8552-8563.
    • (2000) J. Org. Chem , vol.65 , pp. 8552-8563
    • Xie, H.1    Shao, Y.2    Becker, J.M.3    Naider, F.4    Gibbs, R.A.5
  • 31
    • 27644439968 scopus 로고    scopus 로고
    • Synthesis of farnesol isomers via a modified Wittig procedure
    • Yu, J. S.; Kleckley, T. S.; Wiemer, D. F. Synthesis of farnesol isomers via a modified Wittig procedure. Org. Lett., 2005, 7, 4803-4806.
    • (2005) Org. Lett , vol.7 , pp. 4803-4806
    • Yu, J.S.1    Kleckley, T.S.2    Wiemer, D.F.3
  • 32
    • 0033603368 scopus 로고    scopus 로고
    • Synthesis of farnesol Analogues through Cu(I)-mediated displacements of allylic THP ethers by grignard reagents
    • Mechelke, M. F. and Wiemer, D. F. Synthesis of farnesol Analogues through Cu(I)-mediated displacements of allylic THP ethers by grignard reagents. J. Org. Chem., 1999, 64, 4821-4829.
    • (1999) J. Org. Chem , vol.64 , pp. 4821-4829
    • Mechelke, M.F.1    Wiemer, D.F.2
  • 34
    • 0014470589 scopus 로고
    • The nature, intergeneric distribution and biosynthesis of isoprenoid quinones and phenols in gram-negative bacteria
    • Whistance, G. R.; Dillon, J. F.; Threlfall, D. R. The nature, intergeneric distribution and biosynthesis of isoprenoid quinones and phenols in gram-negative bacteria. Biochem. J., 1969, 111, 461-472.
    • (1969) Biochem. J , vol.111 , pp. 461-472
    • Whistance, G.R.1    Dillon, J.F.2    Threlfall, D.R.3
  • 35
    • 0035949539 scopus 로고    scopus 로고
    • Ubiquinone biosynthesis in microorganisms
    • Meganathan, R. Ubiquinone biosynthesis in microorganisms. FEMS Microbiol. Lett., 2001, 203, 131-139.
    • (2001) FEMS Microbiol. Lett , vol.203 , pp. 131-139
    • Meganathan, R.1
  • 36
    • 67749089506 scopus 로고    scopus 로고
    • Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms
    • Kawamukai, M. Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms. Biotechnol. Appl. Biochem., 2009, 53, 217-226.
    • (2009) Biotechnol. Appl. Biochem , vol.53 , pp. 217-226
    • Kawamukai, M.1
  • 37
    • 0032843484 scopus 로고    scopus 로고
    • Microbial ubiquinones: Multiple roles in respiration, gene regulation and oxidative stress management
    • Soballe, B. and Poole, R. K. Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management. Microbiology, 1999, 145 (Pt 8), 1817-1830.
    • (1999) Microbiology , vol.145 , Issue.Pt 8 , pp. 1817-1830
    • Soballe, B.1    Poole, R.K.2
  • 38
    • 0028180730 scopus 로고
    • Characterization of polyprenyldiphosphate: 4-hydroxybenzoate polyprenyltransferase from Escherichia coli
    • Melzer, M. and Heide, L. Characterization of polyprenyldiphosphate: 4-hydroxybenzoate polyprenyltransferase from Escherichia coli. Biochim. Biophys. Acta, 1994, 1212, 93-102.
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 93-102
    • Melzer, M.1    Heide, L.2
  • 39
    • 0031001582 scopus 로고    scopus 로고
    • The ispB gene encoding octaprenyl diphosphate synthase is essential for growth of Escherichia coli
    • Okada, K.; Minehira, M.; Zhu, X.; Suzuki, K.; Nakagawa, T.; Matsuda, H.; Kawamukai, M. The ispB gene encoding octaprenyl diphosphate synthase is essential for growth of Escherichia coli. J. Bacteriol., 1997, 179, 3058-3060.
    • (1997) J. Bacteriol , vol.179 , pp. 3058-3060
    • Okada, K.1    Minehira, M.2    Zhu, X.3    Suzuki, K.4    Nakagawa, T.5    Matsuda, H.6    Kawamukai, M.7
  • 40
    • 0035896537 scopus 로고    scopus 로고
    • Dimer formation of octaprenyl-diphosphate synthase (IspB) is essential for chain length determination of ubiquinone
    • Kainou, T.; Okada, K.; Suzuki, K.; Nakagawa, T.; Matsuda, H.; Kawamukai, M. Dimer formation of octaprenyl-diphosphate synthase (IspB) is essential for chain length determination of ubiquinone. J. Biol. Chem., 2001, 276, 7876-7883.
    • (2001) J. Biol. Chem , vol.276 , pp. 7876-7883
    • Kainou, T.1    Okada, K.2    Suzuki, K.3    Nakagawa, T.4    Matsuda, H.5    Kawamukai, M.6
  • 41
    • 0015869326 scopus 로고
    • The use of mutants of Escherichia coli K12 in studying electron transport and oxidative phosphorylation
    • Gibson, F. and Cox, G. B. The use of mutants of Escherichia coli K12 in studying electron transport and oxidative phosphorylation. Essays Biochem., 1973, 9, 1-29.
    • (1973) Essays Biochem , vol.9 , pp. 1-29
    • Gibson, F.1    Cox, G.B.2
  • 42
    • 0026754531 scopus 로고
    • Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes
    • Daniels, D. L.; Plunkett, G., 3rd; Burland, V.; Blattner, F. R. Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes. Science, 1992, 257, 771-778.
    • (1992) Science , vol.257 , pp. 771-778
    • Daniels, D.L.1    Plunkett 3rd, G.2    Burland, V.3    Blattner, F.R.4
  • 43
    • 0015607502 scopus 로고
    • Pathway for ubiquinone biosynthesis in Escherichia coli K-12: Gene-enzyme relationships and intermediates
    • Young, I. G.; Stroobant, P.; Macdonald, C. G.; Gibson, F. Pathway for ubiquinone biosynthesis in Escherichia coli K-12: gene-enzyme relationships and intermediates. J. Bacteriol., 1973, 114, 42-52.
    • (1973) J. Bacteriol , vol.114 , pp. 42-52
    • Young, I.G.1    Stroobant, P.2    Macdonald, C.G.3    Gibson, F.4
  • 44
    • 68549094464 scopus 로고    scopus 로고
    • An alternative menaquinone biosynthetic pathway operating in microorganisms: An attractive target for drug discovery to pathogenic Helicobacter and Chlamydia strains
    • (Tokyo)
    • Dairi, T. An alternative menaquinone biosynthetic pathway operating in microorganisms: an attractive target for drug discovery to pathogenic Helicobacter and Chlamydia strains. J. Antibiot., (Tokyo) 2009, 62, 347-352.
    • (2009) J. Antibiot , vol.62 , pp. 347-352
    • Dairi, T.1
  • 45
    • 0035219809 scopus 로고    scopus 로고
    • Biosynthesis of menaquinone (vitamin K2) and ubiquinone (coenzyme Q): A perspective on enzymatic mechanisms
    • Meganathan, R. Biosynthesis of menaquinone (vitamin K2) and ubiquinone (coenzyme Q): a perspective on enzymatic mechanisms. Vitam. Horm., 2001, 61, 173-218.
    • (2001) Vitam. Horm , vol.61 , pp. 173-218
    • Meganathan, R.1
  • 46
    • 56949084464 scopus 로고    scopus 로고
    • Specificity and reactivity in menaquinone biosynthesis: The structure of Escherichia coli MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1- carboxylate synthase)
    • Dawson, A.; Fyfe, P. K.; Hunter, W. N. Specificity and reactivity in menaquinone biosynthesis: the structure of Escherichia coli MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1- carboxylate synthase). J. Mol. Biol., 2008, 384, 1353-1368.
    • (2008) J. Mol. Biol , vol.384 , pp. 1353-1368
    • Dawson, A.1    Fyfe, P.K.2    Hunter, W.N.3
  • 47
    • 0020455368 scopus 로고
    • Characterization of Escherichia coli men mutants defective in conversion of o-succinylbenzoate to 1,4-dihydroxy-2-naphthoate
    • Shaw, D. J.; Guest, J. R.; Meganathan, R.; Bentley, R. Characterization of Escherichia coli men mutants defective in conversion of o-succinylbenzoate to 1,4-dihydroxy-2-naphthoate. J. Bacteriol., 1982, 152, 1132-1137.
    • (1982) J. Bacteriol , vol.152 , pp. 1132-1137
    • Shaw, D.J.1    Guest, J.R.2    Meganathan, R.3    Bentley, R.4
  • 48
    • 0031596770 scopus 로고    scopus 로고
    • Menaquinone (Vitamin K2) biosynthesis: Localization and characterization of the menA gene from Escherichia coli
    • Suvarna, K.; Stevenson, D.; Meganathan, R.; Hudspeth, M. E. S. Menaquinone (Vitamin K2) biosynthesis: Localization and characterization of the menA gene from Escherichia coli. J. Bacteriol., 1998, 180, 2782-2787.
    • (1998) J. Bacteriol , vol.180 , pp. 2782-2787
    • Suvarna, K.1    Stevenson, D.2    Meganathan, R.3    Hudspeth, M.E.S.4
  • 49
    • 0030992769 scopus 로고    scopus 로고
    • Identification of a novel gene cluster participating in menaquinone (vitamin K2) biosynthesis. Cloning and sequence determination of the 2- heptaprenyl-1,4-naphthoquinone methyltransferase gene of Bacillus stearothermophilus
    • Koike-Takeshita, A.; Koyama, T.; Ogura, K. Identification of a novel gene cluster participating in menaquinone (vitamin K2) biosynthesis. Cloning and sequence determination of the 2- heptaprenyl-1,4-naphthoquinone methyltransferase gene of Bacillus stearothermophilus. J. Biol. Chem., 1997, 272, 12380-12383.
    • (1997) J. Biol. Chem , vol.272 , pp. 12380-12383
    • Koike-Takeshita, A.1    Koyama, T.2    Ogura, K.3
  • 50
    • 0025365339 scopus 로고
    • Linkage map of Escherichia coli K-12, edition 8
    • Bachmann, B. J. Linkage map of Escherichia coli K-12, edition 8. Microbiol. Rev., 1990, 54, 130-197.
    • (1990) Microbiol. Rev , vol.54 , pp. 130-197
    • Bachmann, B.J.1
  • 51
    • 0018884545 scopus 로고
    • Linkage map of Escherichia coli K-12, edition 6
    • Bachmann, B. J. and Low, K. B. Linkage map of Escherichia coli K-12, edition 6. Microbiol. Rev., 1980, 44, 1-56.
    • (1980) Microbiol. Rev , vol.44 , pp. 1-56
    • Bachmann, B.J.1    Low, K.B.2
  • 52
    • 0031670734 scopus 로고    scopus 로고
    • Linkage map of Escherichia coli K-12, edition 10: The traditional map
    • Berlyn, M. K. B. Linkage map of Escherichia coli K-12, edition 10: the traditional map. Microbiol. Mol. Biol. Rev. 1998, 62, 814-984.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , pp. 814-984
    • Berlyn, M.K.B.1
  • 53
    • 0018603535 scopus 로고
    • Anaerobic growth of Escherichia coli K12 with fumarate as terminal electron acceptor. Genetic studies with menaquinone and fluoroacetate-resistant mutants
    • Guest, J. R. Anaerobic growth of Escherichia coli K12 with fumarate as terminal electron acceptor. Genetic studies with menaquinone and fluoroacetate-resistant mutants. J. Gen. Microbiol. 1979, 115, 259-271.
    • (1979) J. Gen. Microbiol , vol.115 , pp. 259-271
    • Guest, J.R.1
  • 54
    • 0031038898 scopus 로고    scopus 로고
    • A Cmethyltransferase involved in both ubiquinone and menaquinone biosynthesis: Isolation and identification of the Escherichia coli ubiE gene
    • Lee, P. T.; Hsu, A. Y.; Ha, H. T.; Clarke, C. F. A Cmethyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene. J. Bacteriol., 1997, 179, 1748-1754.
    • (1997) J. Bacteriol , vol.179 , pp. 1748-1754
    • Lee, P.T.1    Hsu, A.Y.2    Ha, H.T.3    Clarke, C.F.4
  • 56
    • 67049119557 scopus 로고    scopus 로고
    • Enzymatic properties of futalosine hydrolase, an enzyme essential to a newly identified menaquinone biosynthetic pathway
    • Hiratsuka, T.; Itoh, N.; Seto, H.; Dairi, T. Enzymatic properties of futalosine hydrolase, an enzyme essential to a newly identified menaquinone biosynthetic pathway. Biosci. Biotechnol. Biochem., 2009, 73, 1137-1141.
    • (2009) Biosci. Biotechnol. Biochem , vol.73 , pp. 1137-1141
    • Hiratsuka, T.1    Itoh, N.2    Seto, H.3    Dairi, T.4
  • 57
    • 77449098362 scopus 로고    scopus 로고
    • Vitamin K and Bone Update. In vivo Metabolism of Vitamin K. - In relation to the conversion of vitamin K(1) to MK-4
    • Okano, T.; Nakagawa, K.; Kamao, M. Vitamin K and Bone Update. In vivo Metabolism of Vitamin K. - In relation to the conversion of vitamin K(1) to MK-4. Clin. Calcium, 2009, 19, 1779-1787.
    • (2009) Clin. Calcium , vol.19 , pp. 1779-1787
    • Okano, T.1    Nakagawa, K.2    Kamao, M.3
  • 58
    • 34248224108 scopus 로고    scopus 로고
    • Geranylgeranyltransferase I as a target for anti-cancer drugs
    • Philips, M. R. and Cox, A. D. Geranylgeranyltransferase I as a target for anti-cancer drugs. J. Clin. Invest, 2007, 117, 1223-1225.
    • (2007) J. Clin. Invest , vol.117 , pp. 1223-1225
    • Philips, M.R.1    Cox, A.D.2
  • 59
    • 1642477902 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors as anticancer agents: Current status
    • Zhu, K.; Hamilton, A. D.; Sebti, S. M. Farnesyltransferase inhibitors as anticancer agents: current status. Curr. Opin. Investig. Drugs, 2003, 4, 1428-1435.
    • (2003) Curr. Opin. Investig. Drugs , vol.4 , pp. 1428-1435
    • Zhu, K.1    Hamilton, A.D.2    Sebti, S.M.3
  • 60
    • 33644858461 scopus 로고    scopus 로고
    • Anti-cancer therapy: Targeting the mevalonate pathway
    • Swanson, K. M. and Hohl, R. J. Anti-cancer therapy: targeting the mevalonate pathway. Curr. Cancer Drug Targets, 2006, 6, 15-37.
    • (2006) Curr. Cancer Drug Targets , vol.6 , pp. 15-37
    • Swanson, K.M.1    Hohl, R.J.2
  • 61
    • 33845232634 scopus 로고    scopus 로고
    • Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations
    • Lopez, L. C.; Schuelke, M.; Quinzii, C. M.; Kanki, T.; Rodenburg, R. J.; Naini, A.; Dimauro, S.; Hirano, M. Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations. Am. J. Hum. Genet., 2006, 79, 1125-1129.
    • (2006) Am. J. Hum. Genet , vol.79 , pp. 1125-1129
    • Lopez, L.C.1    Schuelke, M.2    Quinzii, C.M.3    Kanki, T.4    Rodenburg, R.J.5    Naini, A.6    Dimauro, S.7    Hirano, M.8
  • 63
    • 1042301374 scopus 로고    scopus 로고
    • Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic Thermotoga maritima and mechanism of product chain length determination
    • Guo, R. T.; Kuo, C. J.; Chou, C. C.; Ko, T. P.; Shr, H. L.; Liang, P. H.; Wang, A. H. Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic Thermotoga maritima and mechanism of product chain length determination. J. Biol. Chem., 2004, 279, 4903-4912.
    • (2004) J. Biol. Chem , vol.279 , pp. 4903-4912
    • Guo, R.T.1    Kuo, C.J.2    Chou, C.C.3    Ko, T.P.4    Shr, H.L.5    Liang, P.H.6    Wang, A.H.7
  • 64
    • 70350230025 scopus 로고    scopus 로고
    • Synergistic effects of chromosomal ispB deletion and dxs overexpression on coenzyme Q(10) production in recombinant Escherichia coli expressing Agrobacterium tumefaciens dps gene
    • Choi, J. H.; Ryu, Y. W.; Park, Y. C.; Seo, J. H. Synergistic effects of chromosomal ispB deletion and dxs overexpression on coenzyme Q(10) production in recombinant Escherichia coli expressing Agrobacterium tumefaciens dps gene. J. Biotechnol., 2009, 144, 64-69.
    • (2009) J. Biotechnol , vol.144 , pp. 64-69
    • Choi, J.H.1    Ryu, Y.W.2    Park, Y.C.3    Seo, J.H.4
  • 65
    • 33845996610 scopus 로고    scopus 로고
    • Residues around the catalytic pocket of DdsA are important for isoprenoids chain elongation
    • Liu, X.; Yuan, Q.; Zhang, H. Residues around the catalytic pocket of DdsA are important for isoprenoids chain elongation. Protein Pept. Lett., 2007, 14, 27-32.
    • (2007) Protein Pept. Lett , vol.14 , pp. 27-32
    • Liu, X.1    Yuan, Q.2    Zhang, H.3
  • 67
    • 28044458534 scopus 로고    scopus 로고
    • Identification, molecular cloning and functional characterization of an octaprenyl pyrophosphate synthase in intra-erythrocytic stages of Plasmodium falciparum
    • Tonhosolo, R.; D'Alexandri, F. L.; Genta, F. A.; Wunderlich, G.; Gozzo, F. C.; Eberlin, M. N.; Peres, V. J.; Kimura, E. A.; Katzin, A. M. Identification, molecular cloning and functional characterization of an octaprenyl pyrophosphate synthase in intra-erythrocytic stages of Plasmodium falciparum. Biochem. J., 2005, 392, 117-126.
    • (2005) Biochem. J , vol.392 , pp. 117-126
    • Tonhosolo, R.1    D'Alexandri, F.L.2    Genta, F.A.3    Wunderlich, G.4    Gozzo, F.C.5    Eberlin, M.N.6    Peres, V.J.7    Kimura, E.A.8    Katzin, A.M.9
  • 69
    • 12344280335 scopus 로고    scopus 로고
    • Synthesis, inhibitory and activation properties of prenyldiphosphate mimics for aromatic prenylations with ubiA-prenyltransferase
    • Zakharova, S.; Fulhorst, M.; Luczak, L.; Wessjohann, L. Synthesis, inhibitory and activation properties of prenyldiphosphate mimics for aromatic prenylations with ubiA-prenyltransferase. Arkivoc, 2004, 79-96.
    • (2004) Arkivoc , pp. 79-96
    • Zakharova, S.1    Fulhorst, M.2    Luczak, L.3    Wessjohann, L.4
  • 70
    • 0031933368 scopus 로고    scopus 로고
    • Stereochemistry- dependent inhibition of RAS farnesylation by farnesyl phosphonic acids
    • Hohl, R. J.; Lewis, K. A.; Cermak, D. M.; Wiemer, D. F. Stereochemistry- dependent inhibition of RAS farnesylation by farnesyl phosphonic acids. Lipids, 1998, 33, 39-46.
    • (1998) Lipids , vol.33 , pp. 39-46
    • Hohl, R.J.1    Lewis, K.A.2    Cermak, D.M.3    Wiemer, D.F.4
  • 73
    • 65349189521 scopus 로고    scopus 로고
    • MenA is a promising drug target for developing novel lead molecules to combat Mycobacterium tuberculosis
    • Kurosu, M.; Crick, D. C. MenA is a promising drug target for developing novel lead molecules to combat Mycobacterium tuberculosis. Med. Chem., 2009, 5, 197-207.
    • (2009) Med. Chem , vol.5 , pp. 197-207
    • Kurosu, M.1    Crick, D.C.2
  • 75
    • 34548118698 scopus 로고    scopus 로고
    • Discovery of 1,4-dihydroxy-2-naphthoate prenyltransferase inhibitors: New drug leads for multidrug-resistant gram-positive pathogens
    • Kurosu, M.; Narayanasamy, P.; Biswas, K.; Dhiman, R.; Crick, D. C. Discovery of 1,4-dihydroxy-2-naphthoate prenyltransferase inhibitors: new drug leads for multidrug-resistant gram-positive pathogens. J. Med. Chem., 2007, 50, 3973-3975.
    • (2007) J. Med. Chem , vol.50 , pp. 3973-3975
    • Kurosu, M.1    Narayanasamy, P.2    Biswas, K.3    Dhiman, R.4    Crick, D.C.5
  • 76
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer, K. H. and Kandler, O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev., 1972, 36, 407-477.
    • (1972) Bacteriol. Rev , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 79
    • 37349041697 scopus 로고    scopus 로고
    • Lipid intermediates in the biosynthesis of bacterial peptidoglycan
    • van Heijenoort, J. Lipid intermediates in the biosynthesis of bacterial peptidoglycan. Microbiol. Mol. Biol. Rev., 2007, 71, 620-635.
    • (2007) Microbiol. Mol. Biol. Rev , vol.71 , pp. 620-635
    • van Heijenoort, J.1
  • 80
    • 33845903833 scopus 로고    scopus 로고
    • Drugs for bad bugs: Confronting the challenges of antibacterial discovery
    • Payne, D. J.; Gwynn, M. N.; Holmes, D. J.; Pompliano, D. L. Drugs for bad bugs: confronting the challenges of antibacterial discovery. Nat. Rev. Drug Discov., 2007, 6, 29-40.
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 29-40
    • Payne, D.J.1    Gwynn, M.N.2    Holmes, D.J.3    Pompliano, D.L.4
  • 82
    • 0023886858 scopus 로고
    • The biological role of dolichol
    • Chojnacki, T. and Dallner, G. The biological role of dolichol. Biochem. J., 1988, 251, 1-9.
    • (1988) Biochem. J , vol.251 , pp. 1-9
    • Chojnacki, T.1    Dallner, G.2
  • 83
    • 0036375597 scopus 로고    scopus 로고
    • Structure, mechanism and function of prenyltransferases
    • Liang, P. H.; Ko, T. P.; Wang, A. H. Structure, mechanism and function of prenyltransferases. Eur. J. Biochem., 2002, 269, 3339-3354.
    • (2002) Eur. J. Biochem , vol.269 , pp. 3339-3354
    • Liang, P.H.1    Ko, T.P.2    Wang, A.H.3
  • 84
    • 0017295250 scopus 로고
    • Prenyltransferase: The mechanism of the reaction
    • Poulter, C. D.; Rilling, H. C. Prenyltransferase: the mechanism of the reaction. Biochemistry, 1976, 15, 1079-1083.
    • (1976) Biochemistry , vol.15 , pp. 1079-1083
    • Poulter, C.D.1    Rilling, H.C.2
  • 85
    • 20144382151 scopus 로고    scopus 로고
    • Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: Roles of the metal ion and conserved residues in catalysis
    • Guo, R. T.; Ko, T. P.; Chen, A. P.; Kuo, C. J.; Wang, A. H.; Liang, P. H. Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J. Biol. Chem., 2005, 280, 20762-20774.
    • (2005) J. Biol. Chem , vol.280 , pp. 20762-20774
    • Guo, R.T.1    Ko, T.P.2    Chen, A.P.3    Kuo, C.J.4    Wang, A.H.5    Liang, P.H.6
  • 86
    • 3142731370 scopus 로고    scopus 로고
    • The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity
    • El Ghachi, M.; Bouhss, A.; Blanot, D.; Mengin-Lecreulx, D. The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity. J. Biol. Chem., 2004, 279, 30106-30113.
    • (2004) J. Biol. Chem , vol.279 , pp. 30106-30113
    • El Ghachi, M.1    Bouhss, A.2    Blanot, D.3    Mengin-Lecreulx, D.4
  • 87
    • 21444450859 scopus 로고    scopus 로고
    • Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli
    • El Ghachi, M.; Derbise, A.; Bouhss, A.; Mengin-Lecreulx, D. Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli. J. Biol. Chem., 2005, 280, 18689-18695.
    • (2005) J. Biol. Chem , vol.280 , pp. 18689-18695
    • El Ghachi, M.1    Derbise, A.2    Bouhss, A.3    Mengin-Lecreulx, D.4
  • 88
    • 0345313624 scopus 로고    scopus 로고
    • Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: Cloning, expression, and characterization of the essential uppS gene
    • Apfel, C. M.; Takacs, B.; Fountoulakis, M.; Stieger, M.; Keck, W. Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene. J. Bacteriol., 1999, 181, 483-492.
    • (1999) J. Bacteriol , vol.181 , pp. 483-492
    • Apfel, C.M.1    Takacs, B.2    Fountoulakis, M.3    Stieger, M.4    Keck, W.5
  • 89
    • 37349106728 scopus 로고    scopus 로고
    • Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate
    • Touze, T.; Tran, A. X.; Hankins, J. V.; Mengin-Lecreulx, D.; Trent, M. S. Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate. Mol. Microbiol., 2008, 67, 264-277.
    • (2008) Mol. Microbiol , vol.67 , pp. 264-277
    • Touze, T.1    Tran, A.X.2    Hankins, J.V.3    Mengin-Lecreulx, D.4    Trent, M.S.5
  • 90
    • 0032935778 scopus 로고    scopus 로고
    • The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol synthesis, is essential for carrier lipid formation in bacterial cell wall synthesis
    • Kato, J.; Fujisaki, S.; Nakajima, K.; Nishimura, Y.; Sato, M.; Nakano, A. The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol synthesis, is essential for carrier lipid formation in bacterial cell wall synthesis. J. Bacteriol., 1999, 181, 2733-2738.
    • (1999) J. Bacteriol , vol.181 , pp. 2733-2738
    • Kato, J.1    Fujisaki, S.2    Nakajima, K.3    Nishimura, Y.4    Sato, M.5    Nakano, A.6
  • 91
    • 34547863963 scopus 로고    scopus 로고
    • An Escherichia coli undecaprenyl-pyrophosphatephosphatase implicated in undecaprenyl phosphate recycling
    • Tatar, L. D.; Marolda, C. L.; Polischuk, A. N.; van Leeuwen, D.; Valvano, M. A. An Escherichia coli undecaprenyl-pyrophosphatephosphatase implicated in undecaprenyl phosphate recycling. Microbiology, 2007, 153, 2518-2529.
    • (2007) Microbiology , vol.153 , pp. 2518-2529
    • Tatar, L.D.1    Marolda, C.L.2    Polischuk, A.N.3    van Leeuwen, D.4    Valvano, M.A.5
  • 92
    • 0031595241 scopus 로고    scopus 로고
    • Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes
    • Mengin-Lecreulx, D.; Ayala, J.; Bouhss, A.; van Heijenoort, J.; Parquet, C.; Hara, H. Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes. J. Bacteriol., 1998, 180, 4406-4412.
    • (1998) J. Bacteriol , vol.180 , pp. 4406-4412
    • Mengin-Lecreulx, D.1    Ayala, J.2    Bouhss, A.3    van Heijenoort, J.4    Parquet, C.5    Hara, H.6
  • 93
    • 0030883565 scopus 로고    scopus 로고
    • A promoter for the first nine genes of the Escherichia coli mra cluster of cell division and cell envelope biosynthesis genes, including ftsI and ftsW
    • Hara, H.; Yasuda, S.; Horiuchi, K.; Park, J. T. A promoter for the first nine genes of the Escherichia coli mra cluster of cell division and cell envelope biosynthesis genes, including ftsI and ftsW. J. Bacteriol., 1997, 179, 5802-5811.
    • (1997) J. Bacteriol , vol.179 , pp. 5802-5811
    • Hara, H.1    Yasuda, S.2    Horiuchi, K.3    Park, J.T.4
  • 94
    • 0025833399 scopus 로고
    • The murG gene of Escherichia coli codes for the UDP-Nacetylglucosamine: N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis
    • Mengin-Lecreulx, D.; Texier, L.; Rousseau, M.; van Heijenoort, J. The murG gene of Escherichia coli codes for the UDP-Nacetylglucosamine: N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis. J. Bacteriol., 1991, 173, 4625-4636.
    • (1991) J. Bacteriol , vol.173 , pp. 4625-4636
    • Mengin-Lecreulx, D.1    Texier, L.2    Rousseau, M.3    van Heijenoort, J.4
  • 95
    • 0031725647 scopus 로고    scopus 로고
    • MraY is an essential gene for cell growth in Escherichia coli
    • Boyle, D. S.; Donachie, W. D. mraY is an essential gene for cell growth in Escherichia coli. J. Bacteriol., 1998, 180, 6429-6432.
    • (1998) J. Bacteriol , vol.180 , pp. 6429-6432
    • Boyle, D.S.1    Donachie, W.D.2
  • 96
    • 23944469901 scopus 로고    scopus 로고
    • Peptidoglycan precursor pools associated with MraY and FtsW deficiencies or antibiotic treatments
    • Lara, B.; Mengin-Lecreulx, D.; Ayala, J. A.; van Heijenoort, J. Peptidoglycan precursor pools associated with MraY and FtsW deficiencies or antibiotic treatments. FEMS Microbiol. Lett., 2005, 250, 195-200.
    • (2005) FEMS Microbiol. Lett , vol.250 , pp. 195-200
    • Lara, B.1    Mengin-Lecreulx, D.2    Ayala, J.A.3    van Heijenoort, J.4
  • 98
    • 0015919863 scopus 로고
    • Complex-Formation between Bacitracin Peptides and Isoprenyl Pyrophosphates - Specificity of Lipid-Peptide Interactions
    • Storm, D. R. and Strominger, J. L. Complex-Formation between Bacitracin Peptides and Isoprenyl Pyrophosphates - Specificity of Lipid-Peptide Interactions. J. Biol. Chem., 1973, 248, 3940-3945.
    • (1973) J. Biol. Chem , vol.248 , pp. 3940-3945
    • Storm, D.R.1    Strominger, J.L.2
  • 99
    • 0000815444 scopus 로고
    • Bacitracin: An inhibitor of the dephosphorylation of lipid pyrophosphate, an intermediate in the biosynthesis of the peptidoglycan of bacterial cell walls
    • Siewert, G.; Strominger, J. L. Bacitracin: An inhibitor of the dephosphorylation of lipid pyrophosphate, an intermediate in the biosynthesis of the peptidoglycan of bacterial cell walls. Proc. Natl. Acad. Sci. USA, 1967, 57, 767-773.
    • (1967) Proc. Natl. Acad. Sci. USA , vol.57 , pp. 767-773
    • Siewert, G.1    Strominger, J.L.2
  • 100
    • 0024498350 scopus 로고
    • Amphomycin inhibits mannosylphosphoryldolichol synthesis by forming a complex with dolichylmonophosphate
    • Banerjee, D. K. Amphomycin inhibits mannosylphosphoryldolichol synthesis by forming a complex with dolichylmonophosphate. J. Biol. Chem., 1989, 264, 2024-2028.
    • (1989) J. Biol. Chem , vol.264 , pp. 2024-2028
    • Banerjee, D.K.1
  • 101
    • 14244265227 scopus 로고    scopus 로고
    • Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthase
    • Chen, A. P.; Chang, S. Y.; Lin, Y. C.; Sun, Y. S.; Chen, C. T.; Wang, A. H.; Liang, P. H. Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthase. Biochem. J., 2005, 386, 169-176.
    • (2005) Biochem. J , vol.386 , pp. 169-176
    • Chen, A.P.1    Chang, S.Y.2    Lin, Y.C.3    Sun, Y.S.4    Chen, C.T.5    Wang, A.H.6    Liang, P.H.7
  • 103
    • 0347298751 scopus 로고    scopus 로고
    • Synthesis and application of a fluorescent substrate analogueto study ligand interactions for undecaprenyl pyrophosphate synthase
    • Chen, A. P.; Chen, Y. H.; Liu, H. P.; Li, Y. C.; Chen, C. T.; Liang, P. H. Synthesis and application of a fluorescent substrate analogueto study ligand interactions for undecaprenyl pyrophosphate synthase. J. Am. Chem. Soc.,2002, 124, 15217-15224.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 15217-15224
    • Chen, A.P.1    Chen, Y.H.2    Liu, H.P.3    Li, Y.C.4    Chen, C.T.5    Liang, P.H.6
  • 104
    • 0842265850 scopus 로고    scopus 로고
    • Synthesis and biological activity of isopentenyl diphosphate analogues
    • Scholte, A. A.; Eubanks, L. M.; Poulter, C. D.; Vederas, J. C. Synthesis and biological activity of isopentenyl diphosphate analogues. Bioorg. Med. Chem., 2004, 12, 763-770.
    • (2004) Bioorg. Med. Chem , vol.12 , pp. 763-770
    • Scholte, A.A.1    Eubanks, L.M.2    Poulter, C.D.3    Vederas, J.C.4
  • 105
    • 40749124827 scopus 로고    scopus 로고
    • Design and structure-activity relationships of potent and selective inhibitors of undecaprenyl pyrophosphate synthase (UPPS): Tetramic, tetronic acids and dihydropyridin-2-ones
    • Peukert, S.; Sun, Y.; Zhang, R.; Hurley, B.; Sabio, M.; Shen, X.; Gray, C.; Dzink-Fox, J.; Tao, J.; Cebula, R.; Wattanasin, S. Design and structure-activity relationships of potent and selective inhibitors of undecaprenyl pyrophosphate synthase (UPPS): tetramic, tetronic acids and dihydropyridin-2-ones. Bioorg. Med. Chem. Lett., 2008, 18, 1840-1844.
    • (2008) Bioorg. Med. Chem. Lett , vol.18 , pp. 1840-1844
    • Peukert, S.1    Sun, Y.2    Zhang, R.3    Hurley, B.4    Sabio, M.5    Shen, X.6    Gray, C.7    Dzink-Fox, J.8    Tao, J.9    Cebula, R.10    Wattanasin, S.11
  • 107
    • 41649106235 scopus 로고    scopus 로고
    • Pivaloyloxymethylmodified isoprenoid bisphosphonates display enhanced inhibition of cellular geranylgeranylation
    • Wiemer, A. J.; Yu, J. S.; Shull, L. W.; Barney, R. J.; Wasko, B. M.; Lamb, K. M.; Hohl, R. J.; Wiemer, D. F. Pivaloyloxymethylmodified isoprenoid bisphosphonates display enhanced inhibition of cellular geranylgeranylation. Bioorg. Med. Chem., 2008, 16, 3652-3660.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 3652-3660
    • Wiemer, A.J.1    Yu, J.S.2    Shull, L.W.3    Barney, R.J.4    Wasko, B.M.5    Lamb, K.M.6    Hohl, R.J.7    Wiemer, D.F.8
  • 108
    • 38049035846 scopus 로고    scopus 로고
    • Mono- and dialkyl isoprenoid bisphosphonates as geranylgeranyl diphosphate synthase inhibitors
    • Wiemer, A. J.; Yu, J. S.; Lamb, K. M.; Hohl, R. J.; Wiemer, D. F. Mono- and dialkyl isoprenoid bisphosphonates as geranylgeranyl diphosphate synthase inhibitors. Bioorg. Med. Chem., 2008, 16, 390-399.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 390-399
    • Wiemer, A.J.1    Yu, J.S.2    Lamb, K.M.3    Hohl, R.J.4    Wiemer, D.F.5
  • 109
    • 33846615517 scopus 로고    scopus 로고
    • Synthesis of fluorescently tagged isoprenoid bisphosphonates that inhibit protein geranylgeranylation
    • Maalouf, M. A.; Wiemer, A. J.; Kuder, C. H.; Hohl, R. J.; Wiemer, D. F. Synthesis of fluorescently tagged isoprenoid bisphosphonates that inhibit protein geranylgeranylation. Bioorg. Med. Chem., 2007, 15, 1959-1966.
    • (2007) Bioorg. Med. Chem , vol.15 , pp. 1959-1966
    • Maalouf, M.A.1    Wiemer, A.J.2    Kuder, C.H.3    Hohl, R.J.4    Wiemer, D.F.5
  • 110
    • 33846131224 scopus 로고    scopus 로고
    • Digeranyl bisphosphonate inhibits geranylgeranyl pyrophosphate synthase
    • Wiemer, A. J.; Tong, H.; Swanson, K. M.; Hohl, R. J. Digeranyl bisphosphonate inhibits geranylgeranyl pyrophosphate synthase. Biochem. Biophys. Res. Commun., 2007, 353, 921-925.
    • (2007) Biochem. Biophys. Res. Commun , vol.353 , pp. 921-925
    • Wiemer, A.J.1    Tong, H.2    Swanson, K.M.3    Hohl, R.J.4
  • 111
    • 33646204998 scopus 로고    scopus 로고
    • Synthesis and biological activity of isoprenoid bisphosphonates
    • Shull, L. W.; Wiemer, A. J.; Hohl, R. J.; Wiemer, D. F. Synthesis and biological activity of isoprenoid bisphosphonates. Bioorg. Med. Chem., 2006, 14, 4130-4136.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 4130-4136
    • Shull, L.W.1    Wiemer, A.J.2    Hohl, R.J.3    Wiemer, D.F.4
  • 115
    • 75449083831 scopus 로고    scopus 로고
    • Mevalonate analogues as substrates of enzymes in the isoprenoid biosynthetic pathway of Streptococcus pneumoniae
    • Kudoh, T.; Park, C. S.; Lefurgy, S. T.; Sun, M.; Michels, T.; Leyh, T. S.; Silverman, R. B. Mevalonate analogues as substrates of enzymes in the isoprenoid biosynthetic pathway of Streptococcus pneumoniae. Bioorg. Med. Chem., 2009, 18(3),1124-1134
    • (2009) Bioorg. Med. Chem , vol.18 , Issue.3 , pp. 1124-1134
    • Kudoh, T.1    Park, C.S.2    Lefurgy, S.T.3    Sun, M.4    Michels, T.5    Leyh, T.S.6    Silverman, R.B.7
  • 116
    • 0024449451 scopus 로고
    • Isolation and characterization of an Escherichia coli mutant having temperature-sensitive farnesyl diphosphate synthase
    • Fujisaki, S.; Nishino, T.; Katsuki, H.; Hara, H.; Nishimura, Y.; Hirota, Y. Isolation and characterization of an Escherichia coli mutant having temperature-sensitive farnesyl diphosphate synthase. J. Bacteriol., 1989, 171, 5654-5658.
    • (1989) J. Bacteriol , vol.171 , pp. 5654-5658
    • Fujisaki, S.1    Nishino, T.2    Katsuki, H.3    Hara, H.4    Nishimura, Y.5    Hirota, Y.6
  • 117
    • 18244366057 scopus 로고    scopus 로고
    • Disruption of the structural gene for farnesyl diphosphate synthase in Escherichia coli
    • Fujisaki, S.; Takahashi, I.; Hara, H.; Horiuchi, K.; Nishino, T.; Nishimura, Y. Disruption of the structural gene for farnesyl diphosphate synthase in Escherichia coli. J. Biochem., 2005, 137, 395-400.
    • (2005) J. Biochem , vol.137 , pp. 395-400
    • Fujisaki, S.1    Takahashi, I.2    Hara, H.3    Horiuchi, K.4    Nishino, T.5    Nishimura, Y.6


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