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Volumn 171, Issue 6, 1999, Pages 371-385

Metabolic state of Zymomonas mobilis in glucose-, fructose-, and xylose- fed continuous cultures as analysed by 13C- and 31P-NMR spectroscopy

Author keywords

13C NMR; Fructose; Glucose; In vivo 31P NMR; Metabolic flux analysis; Rate limiting step; Sugar phosphates; Xylose; Zymomonas mobilis

Indexed keywords

FRUCTOSE; FRUCTOSE 6 PHOSPHATE; GLUCOSE; XYLOSE;

EID: 0032981109     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050724     Document Type: Article
Times cited : (78)

References (49)
  • 1
    • 0021792109 scopus 로고
    • Studies on cell-free metabolism: Ethanol production by extracts of Zymomonas mobilis
    • Algar EM, Scopes RK (1985) Studies on cell-free metabolism: ethanol production by extracts of Zymomonas mobilis. J Biotechnol 2:275-287
    • (1985) J Biotechnol , vol.2 , pp. 275-287
    • Algar, E.M.1    Scopes, R.K.2
  • 2
    • 0021956712 scopus 로고
    • Regulation of glucose-6-phosphate dehydrogenase in Zymomonas mobilis CP4
    • Anderson AJ, Dawes EA (1985) Regulation of glucose-6-phosphate dehydrogenase in Zymomonas mobilis CP4. FEMS Microbiol Lett 27:23-27
    • (1985) FEMS Microbiol Lett , vol.27 , pp. 23-27
    • Anderson, A.J.1    Dawes, E.A.2
  • 4
    • 0000374729 scopus 로고
    • Junctions of catabolic and anabolic pathways in Zymomonas mobilis: Phosphoenolpyruvate carboxylase and malic enzyme
    • Bringer-Meyer S, Sahm H (1989) Junctions of catabolic and anabolic pathways in Zymomonas mobilis: phosphoenolpyruvate carboxylase and malic enzyme. Appl Microbiol Biotechnol 31: 529-536
    • (1989) Appl Microbiol Biotechnol , vol.31 , pp. 529-536
    • Bringer-Meyer, S.1    Sahm, H.2
  • 5
    • 0027499093 scopus 로고
    • Formation of acetyl-CoA in Zymomonas mobilia by a pyruvate dehydrogenase complex
    • Bringer-Meyer S, Sahm H (1993) Formation of acetyl-CoA in Zymomonas mobilia by a pyruvate dehydrogenase complex. Arch Microbiol 159:197-199
    • (1993) Arch Microbiol , vol.159 , pp. 197-199
    • Bringer-Meyer, S.1    Sahm, H.2
  • 6
    • 0014709653 scopus 로고
    • Effect of starvation on the viability and cellular constituents of Zymomonas anaerobia and Zymomonas mobilis
    • Dawes EA, Large PJ (1970) Effect of starvation on the viability and cellular constituents of Zymomonas anaerobia and Zymomonas mobilis. J Gen Microbiol 60:31-42
    • (1970) J Gen Microbiol , vol.60 , pp. 31-42
    • Dawes, E.A.1    Large, P.J.2
  • 7
    • 0013888124 scopus 로고
    • Sucrose utilization by Zymomonas mobilis: Formation of a levan
    • Dawes EA, Ribbons DW (1966) Sucrose utilization by Zymomonas mobilis: formation of a levan. Biochem J 98:804-812
    • (1966) Biochem J , vol.98 , pp. 804-812
    • Dawes, E.A.1    Ribbons, D.W.2
  • 8
    • 0013571683 scopus 로고
    • Final technical report (December 1970) for contract no. DAJA 37-67-C-0567, European Research Office, US Army
    • Dawes EA, Midgley M, Ishaq M (1970) The endogenous metabolism of anaerobic bacteria. Final technical report (December 1970) for contract no. DAJA 37-67-C-0567, European Research Office, US Army
    • (1970) The Endogenous Metabolism of Anaerobic Bacteria
    • Dawes, E.A.1    Midgley, M.2    Ishaq, M.3
  • 9
    • 0000943064 scopus 로고
    • Continuous-flow NMR bioreactor for in vivo studies ofmicrobial cell suspensions with low biomass concentrations
    • De Graaf AA, Wittig RM, Probst U, Strohhäcker J, Schoberth SM, Sahm H (1992) Continuous-flow NMR bioreactor for in vivo studies ofmicrobial cell suspensions with low biomass concentrations. J Magn Reson Imaging 98:654-659
    • (1992) J Magn Reson Imaging , vol.98 , pp. 654-659
    • De Graaf, A.A.1    Wittig, R.M.2    Probst, U.3    Strohhäcker, J.4    Schoberth, S.M.5    Sahm, H.6
  • 10
    • 0026451207 scopus 로고
    • Pentose metabolism in Zymomonas mobilia wild-type and recombinant strains
    • Feldmann SD, Sahm H, Sprenger GA (1992a) Pentose metabolism in Zymomonas mobilia wild-type and recombinant strains. Appl Microbiol Biotechnol 38:354-361
    • (1992) Appl Microbiol Biotechnol , vol.38 , pp. 354-361
    • Feldmann, S.D.1    Sahm, H.2    Sprenger, G.A.3
  • 11
    • 0026731714 scopus 로고
    • Cloning and expression of the genes for xylose isomerase and xylulokinase from Klebsiella pneumoniae 1033 in Escherichia coli K-12
    • Feldmann SD, Sahm H, Sprenger GA (1992b) Cloning and expression of the genes for xylose isomerase and xylulokinase from Klebsiella pneumoniae 1033 in Escherichia coli K-12. Mol Gen Genet 234:201-210
    • (1992) Mol Gen Genet , vol.234 , pp. 201-210
    • Feldmann, S.D.1    Sahm, H.2    Sprenger, G.A.3
  • 13
    • 9444269228 scopus 로고    scopus 로고
    • Development and application of a membrane cyclone reactor for in vivo NMR spectroscopy with high microbial cell densities
    • Hartbrich A, Schmitz G, Weuster-Botz D, De Graaf AA, Wandrey C (1996) Development and application of a membrane cyclone reactor for in vivo NMR spectroscopy with high microbial cell densities. Biotechnol Bioeng 51:624-635
    • (1996) Biotechnol Bioeng , vol.51 , pp. 624-635
    • Hartbrich, A.1    Schmitz, G.2    Weuster-Botz, D.3    De Graaf, A.A.4    Wandrey, C.5
  • 14
    • 0028228634 scopus 로고
    • Enzymes involved in the formation of glycerol-3-phosphate and the by-products dihydroxyacetone and glycerol in Zymomonas mobilia
    • Horbach S, Strohhäcker J, Welle R, De Graaf AA, Sahm H (1994) Enzymes involved in the formation of glycerol-3-phosphate and the by-products dihydroxyacetone and glycerol in Zymomonas mobilia. FEMS Microbiol Lett 120:37-44
    • (1994) FEMS Microbiol Lett , vol.120 , pp. 37-44
    • Horbach, S.1    Strohhäcker, J.2    Welle, R.3    De Graaf, A.A.4    Sahm, H.5
  • 17
    • 0021138828 scopus 로고
    • The macromolecular composition and essential amino acid profiles of strains of Zymomonas mobilis
    • Low KS, Rogers PL (1984) The macromolecular composition and essential amino acid profiles of strains of Zymomonas mobilis. Appl Microbiol Biotechnol 19:75-78
    • (1984) Appl Microbiol Biotechnol , vol.19 , pp. 75-78
    • Low, K.S.1    Rogers, P.L.2
  • 18
    • 0030050268 scopus 로고    scopus 로고
    • Determination of the fluxes in the central metabolism of Corynebacterium glutamicum by NMR spectroscopy combined with metabolite balancing
    • Maxx A, De Graaf AA, Wiechert W, Eggeling L, Sahm H (1996) Determination of the fluxes in the central metabolism of Corynebacterium glutamicum by NMR spectroscopy combined with metabolite balancing. Biotechnol Bioeng 49:111-129
    • (1996) Biotechnol Bioeng , vol.49 , pp. 111-129
    • Maxx, A.1    De Graaf, A.A.2    Wiechert, W.3    Eggeling, L.4    Sahm, H.5
  • 19
    • 0030609285 scopus 로고    scopus 로고
    • Response of the central metabolism of Corynebacterium glutamicum to different flux burdens
    • Maxx A, Striegel K, De Graaf AA, Sahm H, Eggeling L (1997) Response of the central metabolism of Corynebacterium glutamicum to different flux burdens. Biotechnol Bioeng 56:168-180
    • (1997) Biotechnol Bioeng , vol.56 , pp. 168-180
    • Maxx, A.1    Striegel, K.2    De Graaf, A.A.3    Sahm, H.4    Eggeling, L.5
  • 20
    • 0032600814 scopus 로고    scopus 로고
    • Response of the central metabolism in Corynebacterium glutamicum to the use of an NADH-dependent glutamate dehydrogenase
    • Marx A, Eikmanns B J, Sahm H, De Graaf AA, Eggeling L (1999) Response of the central metabolism in Corynebacterium glutamicum to the use of an NADH-dependent glutamate dehydrogenase. Metab Eng 1:35-48
    • (1999) Metab Eng , vol.1 , pp. 35-48
    • Marx, A.1    Eikmanns, B.J.2    Sahm, H.3    De Graaf, A.A.4    Eggeling, L.5
  • 22
    • 0023050194 scopus 로고
    • Isolation and properties of the glycolytic enzymes from Zymomonas mobilis. The five enzymes from glyceraldehyde-3-phosphate dehydrogenase through to pyruvate kinase
    • Pawluk A., Scopes RK, Griffiths-Smith K (1986) Isolation and properties of the glycolytic enzymes from Zymomonas mobilis. The five enzymes from glyceraldehyde-3-phosphate dehydrogenase through to pyruvate kinase. Biochem J 238:275-81
    • (1986) Biochem J , vol.238 , pp. 275-281
    • Pawluk, A.1    Scopes, R.K.2    Griffiths-Smith, K.3
  • 23
    • 0028817559 scopus 로고
    • Zymomonas mobilia squalene-hopene cyclase gene (shc): Cloning DNA sequence analysis, and expression in Escherichia coli
    • Reipen IG, Poralla K, Sahm H, Sprenger GA (1995) Zymomonas mobilia squalene-hopene cyclase gene (shc): cloning, DNA sequence analysis, and expression in Escherichia coli. Microbiology 141:155-161
    • (1995) Microbiology , vol.141 , pp. 155-161
    • Reipen, I.G.1    Poralla, K.2    Sahm, H.3    Sprenger, G.A.4
  • 26
    • 0027336129 scopus 로고
    • 13C nuclear magnetic resonance spectroscopy to follow sugar uptake in Zymomonas mobilis
    • 13C nuclear magnetic resonance spectroscopy to follow sugar uptake in Zymomonas mobilis. Anal Biochem 210:123-128
    • (1993) Anal Biochem , vol.210 , pp. 123-128
    • Schoberth, S.M.1    De Graaf, A.A.2
  • 27
    • 0030821701 scopus 로고    scopus 로고
    • Allosteric control of Zymomonas mobilis glucose-6-phosphate dehydrogenase by phosphoenolpyruvate
    • Scopes RK (1997) Allosteric control of Zymomonas mobilis glucose-6-phosphate dehydrogenase by phosphoenolpyruvate. Biochem J 326:731-735
    • (1997) Biochem J , vol.326 , pp. 731-735
    • Scopes, R.K.1
  • 28
    • 0021382383 scopus 로고
    • Use of differential dye-ligand chromatography with affinity elution for enzyme purification: 6-Phosphogluconate dehydratase from Zymomonas mobilis
    • Scopes RK, Griffiths-Smith K (1984) Use of differential dye-ligand chromatography with affinity elution for enzyme purification: 6-phosphogluconate dehydratase from Zymomonas mobilis. Anal Biochem 136:530-534
    • (1984) Anal Biochem , vol.136 , pp. 530-534
    • Scopes, R.K.1    Griffiths-Smith, K.2
  • 29
    • 0021800354 scopus 로고
    • Simultaneous purification and characterization of glucokinase, fructokinase and glucose-6-phosphate dehydrogenase from Zymomonas mobilis
    • Scopes RK, Testolin V, Stoter A, Griffiths-Smith K, Algar EM (1985) Simultaneous purification and characterization of glucokinase, fructokinase and glucose-6-phosphate dehydrogenase from Zymomonas mobilis. Biochem J 228:627-634
    • (1985) Biochem J , vol.228 , pp. 627-634
    • Scopes, R.K.1    Testolin, V.2    Stoter, A.3    Griffiths-Smith, K.4    Algar, E.M.5
  • 30
    • 0002433715 scopus 로고
    • Vector plasmids for in vivo and in vitro manipulations of gram-negative bacteria
    • Pühler A (ed). Springer, Berlin Heidelberg New York
    • Simon R, Priefer U, Pühler A (1983) Vector plasmids for in vivo and in vitro manipulations of gram-negative bacteria. In: Pühler A (ed) Molecular genetics of the bacteria-plant interaction. Springer, Berlin Heidelberg New York, pp 98-106
    • (1983) Molecular Genetics of the Bacteria-Plant Interaction , pp. 98-106
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 31
  • 32
    • 0030589557 scopus 로고    scopus 로고
    • Carbohydrate metabolism in Zymomonas mobilis: A catabolic highway with some scenic routes
    • Sprenger GA (1996) Carbohydrate metabolism in Zymomonas mobilis: a catabolic highway with some scenic routes. FEMS Microbiol Lett 145:301-307
    • (1996) FEMS Microbiol Lett , vol.145 , pp. 301-307
    • Sprenger, G.A.1
  • 33
    • 0029067816 scopus 로고
    • Transketolase A of Escherichia coli K-12. Purification and properties of the enzyme from recombinant strains
    • Sprenger GA, Schörken U, Sprenger G, Sahm H (1995a) Transketolase A of Escherichia coli K-12. Purification and properties of the enzyme from recombinant strains. Eur J Biochem 230:525-532
    • (1995) Eur J Biochem , vol.230 , pp. 525-532
    • Sprenger, G.A.1    Schörken, U.2    Sprenger, G.3    Sahm, H.4
  • 34
    • 0028862915 scopus 로고
    • Transaldolase B of Escherichia coli K-12: Cloning of its gene, talB, and characterization of the enzyme from recombinant strains
    • Sprenger GA, Schörken U, Sprenger G, Sahm H (1995b) Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains. J Bacteriol 177:5930-5936
    • (1995) J Bacteriol , vol.177 , pp. 5930-5936
    • Sprenger, G.A.1    Schörken, U.2    Sprenger, G.3    Sahm, H.4
  • 38
    • 0017361914 scopus 로고
    • The biology of Zymomonas
    • Swings J, De Ley J (1977) The biology of Zymomonas. Bacteriol Rev 41:1-46
    • (1977) Bacteriol Rev , vol.41 , pp. 1-46
    • Swings, J.1    De Ley, J.2
  • 39
    • 0001389155 scopus 로고
    • Transaldolase
    • Boyer PD (ed). Academic Press, New York
    • Tsolas O, Horecker BL (1972) Transaldolase. In: Boyer PD (ed) The enzymes, 3rd edn, vol 7. Academic Press, New York, pp 259-280
    • (1972) The Enzymes, 3rd Edn. , vol.7 , pp. 259-280
    • Tsolas, O.1    Horecker, B.L.2
  • 40
    • 0001586925 scopus 로고
    • Carbohydrate metabolism in Zymomonas
    • Viikari L (1988) Carbohydrate metabolism in Zymomonas. Crit Rev Biotechnol 7:237-261
    • (1988) Crit Rev Biotechnol , vol.7 , pp. 237-261
    • Viikari, L.1
  • 41
  • 42
    • 0029011965 scopus 로고
    • Functional expression of the glucose transporter of Zymomonas mobilis leads to restoration of glucose and fructose uptake in Escherichia coli mutants and provides evidence for its facilitator action
    • Weisser P, Krämer R, Sahm H, Sprenger GA (1995) Functional expression of the glucose transporter of Zymomonas mobilis leads to restoration of glucose and fructose uptake in Escherichia coli mutants and provides evidence for its facilitator action. J Bacteriol 177:3351-3354
    • (1995) J Bacteriol , vol.177 , pp. 3351-3354
    • Weisser, P.1    Krämer, R.2    Sahm, H.3    Sprenger, G.A.4
  • 43
    • 0029834422 scopus 로고    scopus 로고
    • Expression of the Escherichia coli pmi gene, encoding phosphomannose-isomerase in Zymomonas mobilis, leads to utilization of mannose as a novel growth substrate, which can be used as a selective marker
    • Weisser P, Krämer R, Sprenger GA (1996) Expression of the Escherichia coli pmi gene, encoding phosphomannose-isomerase in Zymomonas mobilis, leads to utilization of mannose as a novel growth substrate, which can be used as a selective marker. Appl Environ Microbiol 62:4155-4161
    • (1996) Appl Environ Microbiol , vol.62 , pp. 4155-4161
    • Weisser, P.1    Krämer, R.2    Sprenger, G.A.3
  • 45
    • 0029687542 scopus 로고    scopus 로고
    • Reaction engineering methods to study intracellular metabolite concentrations
    • Scheper T (ed). Springer, Berlin Heidelberg New York
    • Weuster-Botz D, De Graaf AA (1996) Reaction engineering methods to study intracellular metabolite concentrations. In: Scheper T (ed) Advances in biochemical engineering/biotechnology, vol 54. Springer, Berlin Heidelberg New York, pp 76 108
    • (1996) Advances in Biochemical Engineering/Biotechnology , vol.54 , pp. 76-108
    • Weuster-Botz, D.1    De Graaf, A.A.2
  • 47
    • 0031554635 scopus 로고    scopus 로고
    • Bidirectional reaction steps in metabolic networks. 1. Modelling and simulation of carbon isotope labelling experiments
    • Wiechert W, De Graaf AA (1997) Bidirectional reaction steps in metabolic networks. 1. Modelling and simulation of carbon isotope labelling experiments. Biotechnol Bioeng 55:101-117
    • (1997) Biotechnol Bioeng , vol.55 , pp. 101-117
    • Wiechert, W.1    De Graaf, A.A.2
  • 48
    • 0031554628 scopus 로고    scopus 로고
    • Bidirectional reaction steps in metabolic networks. 2. Flux estimation and statistical analysis
    • Wiechert W, Siefke C, De Graaf AA, Marx A (1997) Bidirectional reaction steps in metabolic networks. 2. Flux estimation and statistical analysis. Biotechnol Bioeng 55:118-135
    • (1997) Biotechnol Bioeng , vol.55 , pp. 118-135
    • Wiechert, W.1    Siefke, C.2    De Graaf, A.A.3    Marx, A.4
  • 49
    • 0028953195 scopus 로고
    • Metabolic engineering of a pentose metabolism pathway in ethanologenic Zymomonas mobilis
    • Zhang M, Eddy C, Deanda K, Finkelstein M, Picataggio S (1995) Metabolic engineering of a pentose metabolism pathway in ethanologenic Zymomonas mobilis. Science 267:240-243
    • (1995) Science , vol.267 , pp. 240-243
    • Zhang, M.1    Eddy, C.2    Deanda, K.3    Finkelstein, M.4    Picataggio, S.5


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