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Volumn 137, Issue 3, 2005, Pages 395-400

Disruption of the structural gene for farnesyl diphosphate synthase in Escherichia coli

Author keywords

Farnesyl diphosphate; Isoprenoid; Menaquinone; Ubiquinone; Undecaprenyl phosphate

Indexed keywords

DIMETHYLALLYLTRANSFERASE; DIMETHYLALYL DIPHOSPHATE; FARSENYL DIPHOSPHATE SYNTHASE; ISOPENTYL DIPHOSPHATE; ISOPRENOID; MENAQUINONE; OCTAPRENYL DIPHOSPHATE; OCTAPRENYL DIPHOSPHATE SYNTHASE; PRENYLAMINE; PYROPHOSPHORIC ACID DERIVATIVE; SYNTHETASE; UBIQUINONE 8; UBIQUINONE DERIVATIVE; UNCLASSIFIED DRUG; UNDECAPRENYL DIPHOSPHATE; UNDECAPRENYL DIPHOSPHATE SYNTHASE; UNDECAPRENYL MONOPHOSPHATE; UNDECAPRENYL PHOSPHATE;

EID: 18244366057     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvi049     Document Type: Article
Times cited : (24)

References (29)
  • 1
    • 11544324496 scopus 로고    scopus 로고
    • Enzymatic aspects of isoprenoid chain elongation
    • Ogura, K. and Koyama, T. (1998) Enzymatic aspects of isoprenoid chain elongation. Chem. Rev. 98, 1263-1276
    • (1998) Chem. Rev. , vol.98 , pp. 1263-1276
    • Ogura, K.1    Koyama, T.2
  • 2
    • 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., and Hirota, Y. (1989) Isolation and characterization of an Escherichia coli mutant having temperature-sensitive farnesyl diphosphate synthase. J. Bacteriol. 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
  • 3
    • 0025696050 scopus 로고
    • Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli
    • Fujisaki, S., Hara, H., Nishimura, Y., Horiuchi, K., and Nishino, T. (1990) Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli. J. Biochem. 108, 995-1000
    • (1990) J. Biochem. , vol.108 , pp. 995-1000
    • Fujisaki, S.1    Hara, H.2    Nishimura, Y.3    Horiuchi, K.4    Nishino, T.5
  • 5
    • 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., and Keck, W. (1999) Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: Cloning, expression, and characterization of the essential uppS gene. J. Bacteriol. 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
  • 6
    • 0032935778 scopus 로고    scopus 로고
    • The Escherichia coli homologue of yeast Rer2, a key enzyme of dolichol synthesis, is essential for the carrier lipid formation in bacterial cell wall synthesis
    • Kato, J., Fujisaki, S., Nakajima, K, Nishimura, Y., Sato, M., and Nakano, A. (1999) The Escherichia coli homologue of yeast Rer2, a key enzyme of dolichol synthesis, is essential for the carrier lipid formation in bacterial cell wall synthesis. J. Bacteriol. 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
  • 7
    • 0022542607 scopus 로고
    • Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis
    • Fujisaki, S., Nishino, T., and Katsuki, H. (1986) Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis. J. Biochem. 99, 1327-1337
    • (1986) J. Biochem. , vol.99 , pp. 1327-1337
    • Fujisaki, S.1    Nishino, T.2    Katsuki, H.3
  • 8
    • 0017394859 scopus 로고
    • Role of quinones in electron transport to oxygen and nitrate in Escherichia coli
    • Wallace, B.J. and Young, I.G. (1977) Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Biochim. Biophys. Acta 461, 84-100
    • (1977) Biochim. Biophys. Acta , vol.461 , pp. 84-100
    • Wallace, B.J.1    Young, I.G.2
  • 9
    • 0015462619 scopus 로고
    • Isolation of the lipid intermediate in peptidoglycan biosynthesis from Escherichia coli
    • Umbreit, J.N. and Strominger, J.L. (1972) Isolation of the lipid intermediate in peptidoglycan biosynthesis from Escherichia coli. J. Bacteriol. 112, 1306-1309
    • (1972) J. Bacteriol. , vol.112 , pp. 1306-1309
    • Umbreit, J.N.1    Strominger, J.L.2
  • 10
    • 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., and Kawamukai, M. (1997) The ispB gene encoding octaprenyl diphosphate synthase is essential for growth of Escherichia coli. J. Bacteriol. 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
  • 11
    • 0019833645 scopus 로고
    • Specific- Purpose plasmid cloning vectors. I. Low copy number, temperature-sensitive, mobilization-defective pSC101-derived containment vectors
    • Hashimoto-Gotoh, T., Franklin, F.C., Nordheim, A., and Timmis, K.N. (1981) Specific- purpose plasmid cloning vectors. I. Low copy number, temperature-sensitive, mobilization-defective pSC101-derived containment vectors. Gene 16, 227-235
    • (1981) Gene , vol.16 , pp. 227-235
    • Hashimoto-Gotoh, T.1    Franklin, F.C.2    Nordheim, A.3    Timmis, K.N.4
  • 12
    • 0025832094 scopus 로고
    • Cloning, mapping, and characterization of Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3
    • Hara, H., Yamamoto, Y., Higashitani, A., Suzuki, H., and Nishimura, Y. (1991) Cloning, mapping, and characterization of Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3. J. Bacteriol. 173, 4799-4813
    • (1991) J. Bacteriol. , vol.173 , pp. 4799-4813
    • Hara, H.1    Yamamoto, Y.2    Higashitani, A.3    Suzuki, H.4    Nishimura, Y.5
  • 13
    • 0000099415 scopus 로고
    • Purification of geranylgeranyl pyrophosphate synthetase from Micrococcus lysodeikticus
    • Kandutsch, A.A., Paulus, H., Levin, E., and Bloch, K. (1964) Purification of geranylgeranyl pyrophosphate synthetase from Micrococcus lysodeikticus. J. Biol. Chem. 239, 2507-2515
    • (1964) J. Biol. Chem. , vol.239 , pp. 2507-2515
    • Kandutsch, A.A.1    Paulus, H.2    Levin, E.3    Bloch, K.4
  • 16
    • 50449147866 scopus 로고
    • Transduction of linked genetic characters of the host by bacteriophage P1
    • Lennox, E.S. (1955) Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1, 190-206
    • (1955) Virology , vol.1 , pp. 190-206
    • Lennox, E.S.1
  • 17
    • 0002802808 scopus 로고
    • Mutants of Escherichia coli requiring methionine and vitamin B12
    • Davis, B.D. and Mingioli, E.S. (1950) Mutants of Escherichia coli requiring methionine and vitamin B12. J. Bacteriol. 60, 17-28
    • (1950) J. Bacteriol. , vol.60 , pp. 17-28
    • Davis, B.D.1    Mingioli, E.S.2
  • 18
    • 0022740187 scopus 로고
    • Direction of travel of RecBC recombinase through bacteriophage lambda DNA
    • Stahl, F.W., Kobayashi, I., Thaler, D., and Stahl, M.M. (1986) Direction of travel of RecBC recombinase through bacteriophage lambda DNA. Genetics 113, 215-227
    • (1986) Genetics , vol.113 , pp. 215-227
    • Stahl, F.W.1    Kobayashi, I.2    Thaler, D.3    Stahl, M.M.4
  • 19
    • 0020627698 scopus 로고
    • Convenient construction of recA deletion derivatives of Escherichia coli
    • Lorence, M.C. and Rupert, C.S. (1983) Convenient construction of recA deletion derivatives of Escherichia coli. J. Bacteriol. 156, 458-459
    • (1983) J. Bacteriol. , vol.156 , pp. 458-459
    • Lorence, M.C.1    Rupert, C.S.2
  • 20
    • 0030696041 scopus 로고    scopus 로고
    • Identification of a thiamine-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., Grolle, S., de Graaf, A.A., Taylor, S.V., Begley, T.P., Bringer-Meyer, S., and Sahm, H. (1997) Identification of a thiamine-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. USA 94, 12857-12862
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12857-12862
    • Sprenger, G.A.1    Schorken, U.2    Wiegert, T.3    Grolle, S.4    De Graaf, A.A.5    Taylor, S.V.6    Begley, T.P.7    Bringer-Meyer, S.8    Sahm, H.9
  • 21
    • 0032478189 scopus 로고    scopus 로고
    • Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis
    • Lois, L.M., Campos, N., Putra, S.R., Danielsen, K., Rohmer, M., and Boronat, A. (1998) Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis. Proc. Natl Acad. Sci. USA 95, 2105-2110
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2105-2110
    • Lois, L.M.1    Campos, N.2    Putra, S.R.3    Danielsen, K.4    Rohmer, M.5    Boronat, A.6
  • 22
    • 0023678371 scopus 로고
    • Determination of isopentenyl diphosphate and farnesyl diphosphate in tissue samples with a comment on secondary regulation of polyisoprenoid biosynthesis
    • Bruenger, E. and Rilling, H.C. (1988) Determination of isopentenyl diphosphate and farnesyl diphosphate in tissue samples with a comment on secondary regulation of polyisoprenoid biosynthesis. Anal. Biochem. 173, 321-327
    • (1988) Anal. Biochem. , vol.173 , pp. 321-327
    • Bruenger, E.1    Rilling, H.C.2
  • 23
    • 0024421915 scopus 로고
    • Inhibition of bacterial isoprenoid synthesis by fosmidomycin, a phosphonic acid-containing antibiotic
    • Shigi, Y. (1989) Inhibition of bacterial isoprenoid synthesis by fosmidomycin, a phosphonic acid-containing antibiotic. J. Antimicob. Chemother. 24, 131-145
    • (1989) J. Antimicob. Chemother. , vol.24 , pp. 131-145
    • Shigi, Y.1
  • 24
    • 0036785228 scopus 로고    scopus 로고
    • Characterization of the depletion of 2-C-methyl-D-erythritol-2, 4-cyclodiphosphate synthase in Escherichia coli and Bacillus subtilis
    • Campbell, T.L. and Brown, E.D. (2002) Characterization of the depletion of 2-C-methyl-D-erythritol-2, 4-cyclodiphosphate synthase in Escherichia coli and Bacillus subtilis. J. Bacteriol. 184, 5609-5618
    • (2002) J. Bacteriol. , vol.184 , pp. 5609-5618
    • Campbell, T.L.1    Brown, E.D.2
  • 26
    • 0027054065 scopus 로고
    • Chain length distribution of the products formed in solanesyl diphosphate synthase reaction
    • Ohnuma, S.-I., Koyama, T., and Ogura, K. (1992) Chain length distribution of the products formed in solanesyl diphosphate synthase reaction. J. Biochem. 112, 743-749
    • (1992) J. Biochem. , vol.112 , pp. 743-749
    • Ohnuma, S.-I.1    Koyama, T.2    Ogura, K.3
  • 27
    • 0026333505 scopus 로고
    • Purification of solanesyl diphosphate synthase from Micrococcus luteus. A new class of prenyltransferase
    • Ohnuma, S.-I., Koyama, T., and Ogura, K. (1991) Purification of solanesyl diphosphate synthase from Micrococcus luteus. A new class of prenyltransferase. J. Biol. Chem. 266, 23706-23713
    • (1991) J. Biol. Chem. , vol.266 , pp. 23706-23713
    • Ohnuma, S.-I.1    Koyama, T.2    Ogura, K.3
  • 28
    • 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., and Kawamukai, M. (2001) Dimer formation of octaprenyl diphosphate synthase (IspB) is essential for chain length determination of ubiquinone. J. Biol. Chem. 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
  • 29
    • 0036479223 scopus 로고    scopus 로고
    • Interaction with the small subunit of geranyl diphosphate synthase modifies the chain length specificity of geranylgeranyl diphosphate synthase to produce geranyl diphosphate
    • Burke, C. and Croteau, R. (2002) Interaction with the small subunit of geranyl diphosphate synthase modifies the chain length specificity of geranylgeranyl diphosphate synthase to produce geranyl diphosphate. J. Biol. Chem. 277, 3141-3149
    • (2002) J. Biol. Chem. , vol.277 , pp. 3141-3149
    • Burke, C.1    Croteau, R.2


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