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Volumn 123, Issue 6, 1998, Pages 1088-1096

Identification of genes affecting lycopene formation in Escherichia coli transformed with carotenoid biosynthetic genes: Candidates for early genes in isoprenoid biosynthesis

Author keywords

Carotenoid; Complement; Escherichia coli; Isoprenoid; Mutant

Indexed keywords

CAROTENOID; ISOPRENOID; LYCOPENE;

EID: 0031780756     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022047     Document Type: Article
Times cited : (37)

References (60)
  • 1
    • 0002254531 scopus 로고
    • Biosynthesis of carotenoids
    • Porter, J.W. and Spurgeon, S.L., eds. John Wiley & Sons, New York
    • Spurgeon, S.L. and Porter, J.W. (1983) Biosynthesis of carotenoids in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 2, pp. 1-122, John Wiley & Sons, New York
    • (1983) Biosynthesis of Isoprenoid Compounds , vol.2 , pp. 1-122
    • Spurgeon, S.L.1    Porter, J.W.2
  • 2
    • 0000679501 scopus 로고
    • Biosynthesis of plant sterols and other triterpenoids
    • Porter, J.W. and Spurgeon, S.L., eds. John Wiley & Sons, New York
    • Goodwin, T.W. (1981) Biosynthesis of plant sterols and other triterpenoids in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 1, pp. 443-480, John Wiley & Sons, New York
    • (1981) Biosynthesis of Isoprenoid Compounds , vol.1 , pp. 443-480
    • Goodwin, T.W.1
  • 3
    • 0001363913 scopus 로고
    • Formation of sterols in animals
    • Porter, J.W. and Spurgeon, S.L., eds. John Wiley & Sons, New York
    • Gaylor, J.L. (1981) Formation of sterols in animals in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 1, pp. 481-544, John Wiley & Sons, New York
    • (1981) Biosynthesis of Isoprenoid Compounds , vol.1 , pp. 481-544
    • Gaylor, J.L.1
  • 4
    • 0000698227 scopus 로고
    • Biosynthesis of ubiquinone and related compounds
    • Porter, J.W. and Spurgeon, S.L., eds. John Wiley & Sons, New York
    • Pennock, J.F. and Threlfall, D.R. (1983) Biosynthesis of ubiquinone and related compounds in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 2, pp. 191-304, John Wiley & Sons, New York
    • (1983) Biosynthesis of Isoprenoid Compounds , vol.2 , pp. 191-304
    • Pennock, J.F.1    Threlfall, D.R.2
  • 5
    • 0000261787 scopus 로고
    • Biosynthesis of monoterpenes
    • Porter, J.W. and Spurgeon, S.L., eds. John Wiley & Sons, New York
    • Croteau, R. (1981) Biosynthesis of monoterpenes in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 1, pp. 225 282, John Wiley & Sons, New York
    • (1981) Biosynthesis of Isoprenoid Compounds , vol.1 , pp. 225282
    • Croteau, R.1
  • 6
    • 0001385198 scopus 로고
    • Biosynthesis of sesquiterpenes
    • Porter, J.W. and Spurgeon, S.L., eds. John Wiley & Sons, New York
    • Cane, D.E. (1981) Biosynthesis of sesquiterpenes in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 1, pp. 283-374, John Wiley & Sons, New York
    • (1981) Biosynthesis of Isoprenoid Compounds , vol.1 , pp. 283-374
    • Cane, D.E.1
  • 7
    • 0000013248 scopus 로고
    • Biosynthesis of diterpenes
    • (Porter, J.W. and Spurgeon, S.L., eds.) John Wiley & Sons, New York
    • West, C.A. (1981) Biosynthesis of diterpenes in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 1, pp. 375 412, John Wiley & Sons, New York
    • (1981) Biosynthesis of Isoprenoid Compounds , vol.1 , pp. 375412
    • West, C.A.1
  • 8
    • 0000428356 scopus 로고
    • Biosynthesis of dolichols and related compounds
    • Porter, J.W. and Spurgeon, S.L., eds. John Wiley & Sons, New York
    • Hemming, F.W. (1983) Biosynthesis of dolichols and related compounds in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 2, pp. 305-354, John Wiley & Sons, New York
    • (1983) Biosynthesis of Isoprenoid Compounds , vol.2 , pp. 305-354
    • Hemming, F.W.1
  • 9
    • 0011821681 scopus 로고
    • Biosynthesis of Rubber
    • Porter, J.W. and Spurgeon, S.L., eds. John Wiley & Sons, New York
    • Benedict, C.R. (1983) Biosynthesis of Rubber in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 2. pp. 355-370, John Wiley & Sons, New York
    • (1983) Biosynthesis of Isoprenoid Compounds , vol.2 , pp. 355-370
    • Benedict, C.R.1
  • 11
    • 0018081814 scopus 로고
    • Mevalonic acid as a precursor of the alkyl sidechain of heme a of cytochrome c oxidase in yeast Saccharomyces cerevisiae
    • Keyhani, J. and Keyhani, E. (1978) Mevalonic acid as a precursor of the alkyl sidechain of heme a of cytochrome c oxidase in yeast Saccharomyces cerevisiae. FEBS Lett. 93, 271-274
    • (1978) FEBS Lett. , vol.93 , pp. 271-274
    • Keyhani, J.1    Keyhani, E.2
  • 12
    • 0023515798 scopus 로고
    • Prokaryotic hopanoids and other polyterpenoid sterol surrogates
    • Ourisson, G., Rohmer, M., and Poralla, K. (1987) Prokaryotic hopanoids and other polyterpenoid sterol surrogates. Annu. Rev. Microbiol. 41, 301-333
    • (1987) Annu. Rev. Microbiol. , vol.41 , pp. 301-333
    • Ourisson, G.1    Rohmer, M.2    Poralla, K.3
  • 13
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke, S. (1992) Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu. Rev. Biochem. 61, 355-386
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 355-386
    • Clarke, S.1
  • 14
    • 0002254531 scopus 로고
    • Conversion of acetyl-coenzyme A to isopentenyl pyrophosphate
    • Porter, J.W. and Spurgeon, S.L., eds. John Wiley & Sons, New York
    • Qureshi, N. and Porter, J.D. (1981) Conversion of acetyl-coenzyme A to isopentenyl pyrophosphate in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 1, pp. 47-94, John Wiley & Sons, New York
    • (1981) Biosynthesis of Isoprenoid Compounds , vol.1 , pp. 47-94
    • Qureshi, N.1    Porter, J.D.2
  • 15
    • 0004199544 scopus 로고
    • Isoprenoid biosynthesis in archaebacteria
    • Porter, J.W. and Spurgeon, S.L., eds. John Wiley & Sons, New York
    • Bu'Lock, J.D., de Rosa, M., and Gambacorta, A. (1983) Isoprenoid biosynthesis in archaebacteria in Biosynthesis of Isoprenoid Compounds (Porter, J.W. and Spurgeon, S.L., eds.) Vol. 2, pp. 159 190, John Wiley & Sons, New York
    • (1983) Biosynthesis of Isoprenoid Compounds , vol.2 , pp. 159190
    • Bu'Lock, J.D.1    De Rosa, M.2    Gambacorta, A.3
  • 17
    • 0022592380 scopus 로고
    • Biosynthesis of isoprenoids in intact cells of Escherichia coli
    • Fujisaki, S., Nishino, T., and Katsuki, H. (1986) Biosynthesis of isoprenoids in intact cells of Escherichia coli. J. Biochem. 99, 1137-1146
    • (1986) J. Biochem. , vol.99 , pp. 1137-1146
    • Fujisaki, S.1    Nishino, T.2    Katsuki, H.3
  • 18
    • 0027234835 scopus 로고
    • Isoprenoid biosynthesis in bacteria: Two different pathways?
    • Horbach, S., Sahm, H., and Welle, R. (1993) Isoprenoid biosynthesis in bacteria: two different pathways? FEMS Microbiol. Lett. 111, 135-140
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 135-140
    • Horbach, S.1    Sahm, H.2    Welle, R.3
  • 20
    • 0024061058 scopus 로고
    • Prokaryotic hopanoids: The biosynthesis of the bacteriohopane skeleton. Formation of isoprenic units from two distinct acetate pools and a novel type of carbon/carbon linkage between a triterpene and D-ribose
    • Flesch, G. and Rohmer, M. (1988) Prokaryotic hopanoids: the biosynthesis of the bacteriohopane skeleton. Formation of isoprenic units from two distinct acetate pools and a novel type of carbon/carbon linkage between a triterpene and D-ribose. Eur. J. Biochem. 175, 405-411
    • (1988) Eur. J. Biochem. , vol.175 , pp. 405-411
    • Flesch, G.1    Rohmer, M.2
  • 21
    • 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., and Sahm, H. (1993) Isoprenoid biosynthesis in bacteria: a novel pathway for the early steps leading to isopentenyl diphosphate. Biochem. J. 295, 517-524
    • (1993) Biochem. J. , vol.295 , pp. 517-524
    • Rohmer, M.1    Knani, M.2    Simonin, P.3    Sutter, B.4    Sahm, H.5
  • 22
    • 0029922877 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate and pyruvate as precursors of isoprenic units in an alternative non-mevalonate pathway for terpenoid biosynthesis
    • Rohmer, M., Seemann, M., Horbach, S., Bringer-Meyer, S., and Sarm, H. (1996) Glyceraldehyde 3-phosphate and pyruvate as precursors of isoprenic units in an alternative non-mevalonate pathway for terpenoid biosynthesis. J. Am. Chem. Soc. 118, 2564-2566
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2564-2566
    • Rohmer, M.1    Seemann, M.2    Horbach, S.3    Bringer-Meyer, S.4    Sarm, H.5
  • 23
    • 0028906885 scopus 로고
    • Some new aspects of isoprenoid biosynthesis in plants a review
    • Bach, T.J. (1995) Some new aspects of isoprenoid biosynthesis in plants a review. Lipids 30, 191-202
    • (1995) Lipids , vol.30 , pp. 191-202
    • Bach, T.J.1
  • 24
    • 0031015862 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoids in higher plant chloroplasts proceeds via a mevalonate-independent pathway
    • Lichtenthaler, H.K., Schwender, J., Disch, A., and Rohmer, M. (1997) Biosynthesis of isoprenoids in higher plant chloroplasts proceeds via a mevalonate-independent pathway. FEBS Lett. 400, 271-274
    • (1997) FEBS Lett. , vol.400 , pp. 271-274
    • Lichtenthaler, H.K.1    Schwender, J.2    Disch, A.3    Rohmer, M.4
  • 25
    • 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., and Rohmer, M. (1996) 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. 316, 73-80
    • (1996) Biochem. J. , vol.316 , pp. 73-80
    • Schwender, J.1    Seemann, M.2    Lichtenthaler, H.K.3    Rohmer, M.4
  • 26
    • 0025871657 scopus 로고
    • Sterol pathway in yeast. Identification and properties of mutant strains defective in mevalonate diphosphate decarboxylase and farnesyl diphosphate synthetase
    • Chambon, C., Ladeveze, V., Servouse, M., Blanchard, L., Javelot, C., Vladescu, B., and Karst, F. (1991) Sterol pathway in yeast. Identification and properties of mutant strains defective in mevalonate diphosphate decarboxylase and farnesyl diphosphate synthetase. Lipids 26, 633-636
    • (1991) Lipids , vol.26 , pp. 633-636
    • Chambon, C.1    Ladeveze, V.2    Servouse, M.3    Blanchard, L.4    Javelot, C.5    Vladescu, B.6    Karst, F.7
  • 27
    • 0025145542 scopus 로고
    • PET genes of Saccharomyces cerevisiae
    • Tzagoloff, A. and Dieckmann, C.L. (1990) PET genes of Saccharomyces cerevisiae. Microbiol. Rev. 54, 211-225
    • (1990) Microbiol. Rev. , vol.54 , pp. 211-225
    • Tzagoloff, A.1    Dieckmann, C.L.2
  • 28
    • 0028158347 scopus 로고
    • A screen for yeast mutants with defects in the dolichol-mediated pathway for N-glycosylation
    • Roos, J., Sternglanz, R., and Lennarz, W.J. (1994) A screen for yeast mutants with defects in the dolichol-mediated pathway for N-glycosylation. Proc. Natl. Acad. Sci. USA 91, 1485-1489
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1485-1489
    • Roos, J.1    Sternglanz, R.2    Lennarz, W.J.3
  • 29
    • 0028906887 scopus 로고
    • Cloning of the late genes in the ergosterol biosynthetic pathway of Saccharomyces cerevisiae - A review
    • Lees, N.D., Skaggs, B., Kirsch, D.R., and Bard, M. (1995) Cloning of the late genes in the ergosterol biosynthetic pathway of Saccharomyces cerevisiae - a review. Lipids 30, 221-226
    • (1995) Lipids , vol.30 , pp. 221-226
    • Lees, N.D.1    Skaggs, B.2    Kirsch, D.R.3    Bard, M.4
  • 30
    • 0025364138 scopus 로고
    • Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase
    • Ashby, M.N. and Edwards, P.A. (1990) Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase. J. Biol. Chem. 265, 13157-13164
    • (1990) J. Biol. Chem. , vol.265 , pp. 13157-13164
    • Ashby, M.N.1    Edwards, P.A.2
  • 31
    • 0026095839 scopus 로고
    • Ubiquinone biosynthesis in Saccharomyces cerevisiae. Isolation and sequence of COQ3, the 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase gene
    • Clarke, C.F., Williams, W., and Teruya, J.H. (1991) Ubiquinone biosynthesis in Saccharomyces cerevisiae. Isolation and sequence of COQ3, the 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase gene. J. Biol. Chem. 266, 16636-16644
    • (1991) J. Biol. Chem. , vol.266 , pp. 16636-16644
    • Clarke, C.F.1    Williams, W.2    Teruya, J.H.3
  • 32
    • 0030063759 scopus 로고    scopus 로고
    • The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for ubiquinone biosynthesis
    • Marbois, B.N. and Clarke, C.F. (1996) The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for ubiquinone biosynthesis. J. Biol. Chem. 271, 2995-3004
    • (1996) J. Biol. Chem. , vol.271 , pp. 2995-3004
    • Marbois, B.N.1    Clarke, C.F.2
  • 33
    • 0030988484 scopus 로고    scopus 로고
    • Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis
    • Barkovich, R.J., Shtanko, A., Shepherd, J.A., Lee, P.T., Myles, D.C., Tzagoloff, A., and Clarke, C.F. (1997) Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis. J. Biol. Chem. 272, 9182-9188
    • (1997) J. Biol. Chem. , vol.272 , pp. 9182-9188
    • Barkovich, R.J.1    Shtanko, A.2    Shepherd, J.A.3    Lee, P.T.4    Myles, D.C.5    Tzagoloff, A.6    Clarke, C.F.7
  • 34
    • 0025977152 scopus 로고
    • Cloning and characterization of ERG8, An essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase
    • Tsay, Y.H. and Robinson, G.W. (1991) Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase. Mol. Cell. Biol. 11, 620-631
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 620-631
    • Tsay, Y.H.1    Robinson, G.W.2
  • 35
    • 0001582965 scopus 로고
    • Chemical and genetic studies on the biosynthesis of ubiquinone by Escherichia coli
    • Gibson, K. (1973) Chemical and genetic studies on the biosynthesis of ubiquinone by Escherichia coli. Biochem. Soc. Trans. 1, 317-327
    • (1973) Biochem. Soc. Trans. , vol.1 , pp. 317-327
    • Gibson, K.1
  • 36
    • 0026775096 scopus 로고
    • Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: The cloning and nucleotide sequence of ubiG. Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases
    • Wu, G., Williams, H.D., Zamanian, M., Gibson, F., and Poole, R.K. (1992) Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: the cloning and nucleotide sequence of ubiG. Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases. J. Gen. Microbiol. 138, 2101-2112
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2101-2112
    • Wu, G.1    Williams, H.D.2    Zamanian, M.3    Gibson, F.4    Poole, R.K.5
  • 37
    • 0027165748 scopus 로고
    • Mutants of Escherichia coli affected in respiration: The cloning and nucleotide sequence of ubiA, encoding the membrane-bound p-hydroxybenzoate:octaprenyltransferase
    • Wu, G., Williams, H.D., Gibson, F., and Poole, R.K. (1993) Mutants of Escherichia coli affected in respiration: the cloning and nucleotide sequence of ubiA, encoding the membrane-bound p-hydroxybenzoate:octaprenyltransferase. J. Gen. Microbiol. 139, 1795-1805
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1795-1805
    • Wu, G.1    Williams, H.D.2    Gibson, F.3    Poole, R.K.4
  • 38
    • 0024341833 scopus 로고
    • Isolation and characterization of isoprene mutants of Escherichia coli
    • Sherman, M.M., Petersen, L.A., and Poulter, C.D. (1989) Isolation and characterization of isoprene mutants of Escherichia coli. J. Bacteriol. 171, 3619-3628
    • (1989) J. Bacteriol. , vol.171 , pp. 3619-3628
    • Sherman, M.M.1    Petersen, L.A.2    Poulter, C.D.3
  • 39
    • 0028283930 scopus 로고
    • Archaebacterial ether-linked lipid biosynthetic gene. Expression cloning, sequencing, and characterization of geranylgeranyl-diphosphate synthase
    • Ohnuma, S.-i., Suzuki, M., and Nishino, T. (1994) Archaebacterial ether-linked lipid biosynthetic gene. Expression cloning, sequencing, and characterization of geranylgeranyl-diphosphate synthase. J. Biol. Chem. 269, 14792-14797
    • (1994) J. Biol. Chem. , vol.269 , pp. 14792-14797
    • Ohnuma, S.-I.1    Suzuki, M.2    Nishino, T.3
  • 40
    • 0025630190 scopus 로고
    • Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by functional analysis of gene products expressed in Escherichia coli
    • Misawa, N., Nakagawa, M., Kobayashi, K., Yamano, S., Izawa, Y., Nakamura, K., and Harashima, K. (1990) Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by functional analysis of gene products expressed in Escherichia coli. J. Bacteriol. 172, 6704-6712
    • (1990) J. Bacteriol. , vol.172 , pp. 6704-6712
    • Misawa, N.1    Nakagawa, M.2    Kobayashi, K.3    Yamano, S.4    Izawa, Y.5    Nakamura, K.6    Harashima, K.7
  • 42
  • 43
    • 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
  • 45
    • 0030048551 scopus 로고    scopus 로고
    • Open reading frame 176 in the photosynthesis gene cluster of Rhodobacter capsulatus encodes idi, A gene for isopentenyl diphosphate isomerase
    • Hahn, F.M., Baker, J.A., and Poulter, C.D. (1996) Open reading frame 176 in the photosynthesis gene cluster of Rhodobacter capsulatus encodes idi, a gene for isopentenyl diphosphate isomerase. J. Bacteriol. 178, 619-624
    • (1996) J. Bacteriol. , vol.178 , pp. 619-624
    • Hahn, F.M.1    Baker, J.A.2    Poulter, C.D.3
  • 46
    • 0021756359 scopus 로고
    • The unc operon. Nucleotide sequence, regulation and structure of ATP-synthase
    • Walker, J.E., Saraste, M., and Gay, N.J. (1984) The unc operon. Nucleotide sequence, regulation and structure of ATP-synthase. Biochim. Biophys. Acta 768, 164-200
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 164-200
    • Walker, J.E.1    Saraste, M.2    Gay, N.J.3
  • 47
    • 0021764887 scopus 로고
    • DNa sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS
    • Walker, J.E., Gay, N.J., Saraste, M., and Eberle, A.N. (1984) DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS. Biochem. J. 224, 799-815
    • (1984) Biochem. J. , vol.224 , pp. 799-815
    • Walker, J.E.1    Gay, N.J.2    Saraste, M.3    Eberle, A.N.4
  • 48
    • 0027434077 scopus 로고
    • Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli
    • Mengin-Lecreulx, D. and van Heijenoort, J. (1993) Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli. J. Bacteriol. 175, 6150-6157
    • (1993) J. Bacteriol. , vol.175 , pp. 6150-6157
    • Mengin-Lecreulx, D.1    Van Heijenoort, J.2
  • 49
    • 0028944586 scopus 로고
    • Ethanol amine utilization in Salmonella typhimurium: Nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster
    • Stojiljkovic, I., Baumler, A.J., and Heffron, F. (1995) Ethanol amine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster. J. Bacteriol. 177, 1357-1366
    • (1995) J. Bacteriol. , vol.177 , pp. 1357-1366
    • Stojiljkovic, I.1    Baumler, A.J.2    Heffron, F.3
  • 50
    • 0021447442 scopus 로고
    • Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12
    • Darlison, M.G., Spencer, M.E., and Guest, J.R. (1984) Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12. Eur. J. Biochem. 141, 351-359
    • (1984) Eur. J. Biochem. , vol.141 , pp. 351-359
    • Darlison, M.G.1    Spencer, M.E.2    Guest, J.R.3
  • 51
    • 0002717720 scopus 로고
    • Complete sequence of the gltA gene encoding citrate synthase in Escherichia coli
    • Ner, S.S., Bhayana, V., Bell, A.W., Giles, I.G., Duckworth H.W., and Bloxham, D.P. (1983) Complete sequence of the gltA gene encoding citrate synthase in Escherichia coli. Biochemistry 22, 5243-5249
    • (1983) Biochemistry , vol.22 , pp. 5243-5249
    • Ner, S.S.1    Bhayana, V.2    Bell, A.W.3    Giles, I.G.4    Duckworth, H.W.5    Bloxham, D.P.6
  • 52
    • 0021451569 scopus 로고
    • Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase
    • Spencer, M.E., Darlison, M.G., Stephens, P.E., Duckenfield, I.K., and Guest, J.R. (1984) Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase. Eur. J. Biochem. 141, 361-374
    • (1984) Eur. J. Biochem. , vol.141 , pp. 361-374
    • Spencer, M.E.1    Darlison, M.G.2    Stephens, P.E.3    Duckenfield, I.K.4    Guest, J.R.5
  • 53
    • 0029010741 scopus 로고
    • aldB, An RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp
    • Xu, J. and Johnson, R.C. (1995) aldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp. J. Bacteriol. 177, 3166-3175
    • (1995) J. Bacteriol. , vol.177 , pp. 3166-3175
    • Xu, J.1    Johnson, R.C.2
  • 54
    • 0025825803 scopus 로고
    • Cloning an Escherichia coli gene encoding a protein remarkably similar to mammalian aldehyde dehydrogenases
    • Heim, R. and Strehler, E.E. (1991) Cloning an Escherichia coli gene encoding a protein remarkably similar to mammalian aldehyde dehydrogenases. Gene 99, 15-23
    • (1991) Gene , vol.99 , pp. 15-23
    • Heim, R.1    Strehler, E.E.2
  • 55
    • 0042212127 scopus 로고    scopus 로고
    • An isochorismate hydroxymutase isogene in Escherichia coli
    • Muller, R., Dahm, C., Schulte, G., and Leistner, E. (1996) An isochorismate hydroxymutase isogene in Escherichia coli. FEBS Lett. 378, 131-134
    • (1996) FEBS Lett. , vol.378 , pp. 131-134
    • Muller, R.1    Dahm, C.2    Schulte, G.3    Leistner, E.4
  • 56
    • 0025815350 scopus 로고
    • Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme
    • Spyrou, G., Haggard-Ljungquist, E., Krook, M., Jornvall, H., Nilsson, E., and Reichard, P. (1991) Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme. J. Bacteriol. 173, 3673-3679
    • (1991) J. Bacteriol. , vol.173 , pp. 3673-3679
    • Spyrou, G.1    Haggard-Ljungquist, E.2    Krook, M.3    Jornvall, H.4    Nilsson, E.5    Reichard, P.6
  • 57
    • 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., and Misawa, N. (1997) Expression of an exogenous isopentenyl diphosphate isomerase gene enhances isoprenoid biosynthesis in Escherichia coli. Biochem. J. 324, 421-426
    • (1997) Biochem. J. , vol.324 , pp. 421-426
    • Kajiwara, S.1    Fraser, P.D.2    Kondo, K.3    Misawa, N.4
  • 58
    • 0018070787 scopus 로고
    • Alternative hydroxylases for the aerobic and anaerobic biosynthesis of ubiquinone in Escherichia coli
    • Alexander, K. and Young, I.G. (1978) Alternative hydroxylases for the aerobic and anaerobic biosynthesis of ubiquinone in Escherichia coli. Biochemistry 17, 4750-4755
    • (1978) Biochemistry , vol.17 , pp. 4750-4755
    • Alexander, K.1    Young, I.G.2
  • 60
    • 0018840227 scopus 로고
    • Microbial metabolism of amino alcohols. Biosynthetic utilization of ethanolamine for lipid synthesis by bacteria
    • Shukla, S.D. and Turner, J.M. (1980) Microbial metabolism of amino alcohols. Biosynthetic utilization of ethanolamine for lipid synthesis by bacteria. Biochem. J. 186, 13-19
    • (1980) Biochem. J. , vol.186 , pp. 13-19
    • Shukla, S.D.1    Turner, J.M.2


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