메뉴 건너뛰기




Volumn 156, Issue 6, 2010, Pages 1860-1872

Metabolic flux analysis of wild-type Escherichia coli and mutants deficient in pyruvate-dissimilating enzymes during the fermentative metabolism of glucuronate

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ACETYL COENZYME A; BACTERIAL ENZYME; FORMATE ACETYLTRANSFERASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUCURONIC ACID; LYASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; PENTOSE PHOSPHATE; PYRUVATE DEHYDROGENASE; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 77953202449     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.036251-0     Document Type: Article
Times cited : (12)

References (49)
  • 1
    • 53049083876 scopus 로고    scopus 로고
    • Metabolic engineering for advanced biofuels production from Escherichia coli
    • Atsumi, S. & Liao, J. C. (2008). Metabolic engineering for advanced biofuels production from Escherichia coli. Curr Opin Biotechnol 19, 414-419.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 414-419
    • Atsumi, S.1    Liao, J.C.2
  • 3
    • 0035856579 scopus 로고    scopus 로고
    • Metabolic flux response to phosphoglucose isomerase knockout in Escherichia coli and impact of overexpression of the soluble transhydrogenase UdhA
    • Canonaco, F., Hess, T. A., Heri, S., Wang, T., Szyperski, T. & Sauer, U. (2001). Metabolic flux response to phosphoglucose isomerase knockout in Escherichia coli and impact of overexpression of the soluble transhydrogenase UdhA. FEMS Microbiol Lett 204, 247-252.
    • (2001) FEMS Microbiol Lett , vol.204 , pp. 247-252
    • Canonaco, F.1    Hess, T.A.2    Heri, S.3    Wang, T.4    Szyperski, T.5    Sauer, U.6
  • 4
    • 0018073799 scopus 로고
    • Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Danson, M. J., Hooper, E. A. & Perham, R. N. (1978). Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Biochem J 175, 193-198. (Pubitemid 9057126)
    • (1978) Biochemical Journal , vol.175 , Issue.1 , pp. 193-198
    • Danson, M.J.1    Hooper, E.A.2    Perham, R.N.3
  • 5
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A. & Wanner, B. L. (2000). One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97, 6640-6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 6
    • 0032906898 scopus 로고    scopus 로고
    • The steady-state internal redox state (NADH/NAD) reflects the external redox state and is correlated with catabolic adaptation in Escherichia coli
    • de Graef, M. R., Alexeeva, S., Snoep, J. L. & Teixeira de Mattos, M. J. (1999). The steady-state internal redox state (NADH/NAD) reflects the external redox state and is correlated with catabolic adaptation in Escherichia coli. J Bacteriol 181, 2351-2357.
    • (1999) J Bacteriol , vol.181 , pp. 2351-2357
    • De Graef, M.R.1    Alexeeva, S.2    Snoep, J.L.3    De Teixeira Mattos, M.J.4
  • 7
    • 15744400448 scopus 로고    scopus 로고
    • A better global resolution function and a novel iterative stochastic search method for optimization of high-performance liquid chromatographic separation
    • Dharmadi, Y. & Gonzalez, R. (2005). A better global resolution function and a novel iterative stochastic search method for optimization of high-performance liquid chromatographic separation. J Chromatogr A 1070, 89-101.
    • (2005) J Chromatogr A , vol.1070 , pp. 89-101
    • Dharmadi, Y.1    Gonzalez, R.2
  • 8
    • 33746868000 scopus 로고    scopus 로고
    • Anaerobic fermentation of glycerol by Escherichia coli: A new platform for metabolic engineering
    • Dharmadi, Y., Murarka, A. & Gonzalez, R. (2006). Anaerobic fermentation of glycerol by Escherichia coli: a new platform for metabolic engineering. Biotechnol Bioeng 94, 821-829.
    • (2006) Biotechnol Bioeng , vol.94 , pp. 821-829
    • Dharmadi, Y.1    Murarka, A.2    Gonzalez, R.3
  • 9
    • 33750290455 scopus 로고    scopus 로고
    • Understanding microbial metabolism
    • Downs, D. M. (2006). Understanding microbial metabolism. Annu Rev Microbiol 60, 533-559.
    • (2006) Annu Rev Microbiol , vol.60 , pp. 533-559
    • Downs, D.M.1
  • 10
    • 0034625143 scopus 로고    scopus 로고
    • The Escherichia coli MG1655 in silico metabolic genotype: Its definition, characteristics, and capabilities
    • Edwards, J. S. & Palsson, B. O. (2000). The Escherichia coli MG1655 in silico metabolic genotype: its definition, characteristics, and capabilities. Proc Natl Acad Sci U S A 97, 5528-5533.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5528-5533
    • Edwards, J.S.1    Palsson, B.O.2
  • 12
    • 64049099490 scopus 로고    scopus 로고
    • Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism
    • Fuhrer, T. & Sauer, U. (2009). Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism. J Bacteriol 191, 2112-2121.
    • (2009) J Bacteriol , vol.191 , pp. 2112-2121
    • Fuhrer, T.1    Sauer, U.2
  • 13
    • 0037457492 scopus 로고    scopus 로고
    • Metabolic analysis of the synthesis of high levels of intracellular human SOD in Saccharomyces cerevisiae rhSOD 2060 411 SGA122
    • Gonzalez, R., Andrews, B. A., Molitor, J. & Asenjo, J. A. (2003). Metabolic analysis of the synthesis of high levels of intracellular human SOD in Saccharomyces cerevisiae rhSOD 2060 411 SGA122. Biotechnol Bioeng 82, 152-169.
    • (2003) Biotechnol Bioeng , vol.82 , pp. 152-169
    • Gonzalez, R.1    Andrews, B.A.2    Molitor, J.3    Asenjo, J.A.4
  • 14
    • 0018603535 scopus 로고
    • Anaerobic growth of Escherichia coli K-12 with fumarate as terminal electron acceptor. Genetic studies with menaquinone and fluoracetate resistant mutants
    • Guest, J. R. (1979). Anaerobic growth of Escherichia coli K-12 with fumarate as terminal electron acceptor. Genetic studies with menaquinone and fluoracetate resistant mutants. J Gen Microbiol 115, 259-271.
    • (1979) J Gen Microbiol , vol.115 , pp. 259-271
    • Guest, J.R.1
  • 15
    • 0024954386 scopus 로고
    • Structure, expression, and protein engineering of the pyruvate dehydrogenase complex of Escherichia coli
    • Guest, J. R., Angier, S. J. & Russell, G. C. (1989). Structure, expression, and protein engineering of the pyruvate dehydrogenase complex of Escherichia coli. Ann N Y Acad Sci 573, 76-99.
    • (1989) Ann N Y Acad Sci , vol.573 , pp. 76-99
    • Guest, J.R.1    Angier, S.J.2    Russell, G.C.3
  • 16
    • 0024349893 scopus 로고
    • Escherichia coli derivatives lacking both alcohol dehydrogenase and phosphotransacetylase grow anaerobically by lactate fermentation
    • Gupta, S. & Clark, D. P. (1989). Escherichia coli derivatives lacking both alcohol dehydrogenase and phosphotransacetylase grow anaerobically by lactate fermentation. J Bacteriol 171, 3650-3655. (Pubitemid 19174135)
    • (1989) Journal of Bacteriology , vol.171 , Issue.7 , pp. 3650-3655
    • Gupta, S.1    Clark, D.P.2
  • 17
    • 7744237727 scopus 로고    scopus 로고
    • Pyruvate formate lyase and acetate kinase are essential for anaerobic growth of Escherichia coli on xylose
    • Hasona, A., Kim, Y., Healy, F. G., Ingram, L. O. & Shanmugam, K. T. (2004). Pyruvate formate lyase and acetate kinase are essential for anaerobic growth of Escherichia coli on xylose. J Bacteriol 186, 7593-7600.
    • (2004) J Bacteriol , vol.186 , pp. 7593-7600
    • Hasona, A.1    Kim, Y.2    Healy, F.G.3    Ingram, L.O.4    Shanmugam, K.T.5
  • 18
    • 0028296342 scopus 로고
    • Pyruvate formate-lyase is not essential for nitrate respiration by Escherichia coli
    • Kaiser, M. & Sawers, G. (1994). Pyruvate formate-lyase is not essential for nitrate respiration by Escherichia coli. FEMS Microbiol Lett 117, 163-168.
    • (1994) FEMS Microbiol Lett , vol.117 , pp. 163-168
    • Kaiser, M.1    Sawers, G.2
  • 21
    • 0031089594 scopus 로고    scopus 로고
    • Fermentation of biomass-derived glucuronic acid by pet expressing recombinants of Escherichia coli B
    • Lawford, H. G. & Rousseau, J. D. (1997). Fermentation of biomass-derived glucuronic acid by pet expressing recombinants of Escherichia coli B. Appl Biochem Biotechnol 63-65, 221-241.
    • (1997) Appl Biochem Biotechnol , vol.63-65 , pp. 221-241
    • Lawford, H.G.1    Rousseau, J.D.2
  • 22
    • 0242475329 scopus 로고    scopus 로고
    • MetaFluxNet: The management of metabolic reaction information and quantitative metabolic flux analysis
    • Lee, D. Y., Yun, H., Park, S. & Lee, S. Y. (2003). MetaFluxNet: the management of metabolic reaction information and quantitative metabolic flux analysis. Bioinformatics 19, 2144-2146.
    • (2003) Bioinformatics , vol.19 , pp. 2144-2146
    • Lee, D.Y.1    Yun, H.2    Park, S.3    Lee, S.Y.4
  • 23
    • 15944366483 scopus 로고    scopus 로고
    • Effect of oxygen on the Escherichia coli ArcA and FNR regulation systems and metabolic responses
    • Levanon, S. S., San, K. Y. & Bennett, G. N. (2005). Effect of oxygen on the Escherichia coli ArcA and FNR regulation systems and metabolic responses. Biotechnol Bioeng 89, 556-564.
    • (2005) Biotechnol Bioeng , vol.89 , pp. 556-564
    • Levanon, S.S.1    San, K.Y.2    Bennett, G.N.3
  • 24
    • 0017414128 scopus 로고
    • Hit-and-run mechanism for D-glucuronate reduction catalyzed by D-mannonate - NAD oxidoreductase of Escherichia coli
    • Mandrand-Berthelot, M. A. & Lagarde, A. E. (1977). Hit-and-run mechanism for D-glucuronate reduction catalyzed by D-mannonate - NAD oxidoreductase of Escherichia coli. Biochim Biophys Acta 483, 6-23.
    • (1977) Biochim Biophys Acta , vol.483 , pp. 6-23
    • Mandrand-Berthelot, M.A.1    Lagarde, A.E.2
  • 26
    • 0024485336 scopus 로고
    • Mutants of Escherichia coli deficient in the fermentative lactate dehydrogenase
    • Mat-Jan, F., Alam, K. Y. & Clark, D. P. (1989). Mutants of Escherichia coli deficient in the fermentative lactate dehydrogenase. J Bacteriol 171, 342-348.
    • (1989) J Bacteriol , vol.171 , pp. 342-348
    • Mat-Jan, F.1    Alam, K.Y.2    Clark, D.P.3
  • 27
  • 28
    • 39649103644 scopus 로고    scopus 로고
    • Fermentative utilization of glycerol in Escherichia coli and its implications for the production of fuels and chemicals
    • Murarka, A., Dharmadi, Y., Yazdani, S. S. & Gonzalez, R. (2008). Fermentative utilization of glycerol in Escherichia coli and its implications for the production of fuels and chemicals. Appl Environ Microbiol 74, 1124-1135.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 1124-1135
    • Murarka, A.1    Dharmadi, Y.2    Yazdani, S.S.3    Gonzalez, R.4
  • 29
  • 32
    • 0347506028 scopus 로고    scopus 로고
    • It is all about metabolic fluxes
    • Nielsen, J. (2003). It is all about metabolic fluxes. J Bacteriol 185, 7031-7035.
    • (2003) J Bacteriol , vol.185 , pp. 7031-7035
    • Nielsen, J.1
  • 33
    • 34249337553 scopus 로고    scopus 로고
    • Biochemical reactions - A first look
    • Edited by J. Nielsen, J. Villadsen and G. Lidén. New York: Springer
    • Nielsen, J., Villadsen, J. & Liden, G. (2003). Biochemical reactions - a first look. In Bioreaction Engineering Principles, pp. 60-73. Edited by J. Nielsen, J. Villadsen and G. Lidén. New York: Springer.
    • (2003) Bioreaction Engineering Principles , pp. 60-73
    • Nielsen, J.1    Villadsen, J.2    Liden, G.3
  • 34
    • 0023390705 scopus 로고
    • Glycolytic flux in Zymomonas mobilis: Enzyme and metabolite levels during batch fermentation
    • Osman, Y. A., Conway, T., Bonetti, S. J. & Ingram, L. O. (1987). Glycolytic flux in Zymomonas mobilis: enzyme and metabolite levels during batch fermentation. J Bacteriol 169, 3726-3736.
    • (1987) J Bacteriol , vol.169 , pp. 3726-3736
    • Osman, Y.A.1    Conway, T.2    Bonetti, S.J.3    Ingram, L.O.4
  • 35
    • 0032464663 scopus 로고    scopus 로고
    • What's for dinner?: Entner-Doudoroff metabolism in Escherichia coli
    • Peekhaus, N. & Conway, T. (1998). What's for dinner?: Entner-Doudoroff metabolism in Escherichia coli. J Bacteriol 180, 3495-3502. (Pubitemid 29115074)
    • (1998) Journal of Bacteriology , vol.180 , Issue.14 , pp. 3495-3502
    • Peekhaus, N.1    Conway, T.2
  • 36
    • 0343035686 scopus 로고    scopus 로고
    • A stoichiometric model of Escherichia coli metabolism: Incorporation of growth-rate dependent biomass composition and mechanistic energy requirements
    • Pramanik, J. & Keasling, J. D. (1997). A stoichiometric model of Escherichia coli metabolism: incorporation of growth-rate dependent biomass composition and mechanistic energy requirements. Biotechnol Bioeng 56, 398-421.
    • (1997) Biotechnol Bioeng , vol.56 , pp. 398-421
    • Pramanik, J.1    Keasling, J.D.2
  • 39
    • 1342325419 scopus 로고    scopus 로고
    • The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli
    • Sauer, U., Canonaco, F., Heri, S., Perrenoud, A. & Fischer, E. (2004). The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J Biol Chem 279, 6613-6619.
    • (2004) J Biol Chem , vol.279 , pp. 6613-6619
    • Sauer, U.1    Canonaco, F.2    Heri, S.3    Perrenoud, A.4    Fischer, E.5
  • 40
    • 33747123465 scopus 로고    scopus 로고
    • Fermentative pyruvate and acetylcoenzyme A metabolism
    • Edited by R. Curtis III. Washington, DC: American Society for Microbiology
    • Sawers, R. G. & Clark, D. P. (2004). Fermentative pyruvate and acetylcoenzyme A metabolism. In EcoSal - Escherichia coli and Salmonella: Cellular and Molecular Biology. Edited by R. Curtis III. Washington, DC: American Society for Microbiology.
    • (2004) EcoSal - Escherichia Coli and Salmonella: Cellular and Molecular Biology
    • Sawers, R.G.1    Clark, D.P.2
  • 41
    • 0021066245 scopus 로고
    • 2-Oxoacid dehydrogenase complexes of Escherichia coli: Cellular amounts and patterns of synthesis
    • Smith, M. W. & Neidhardt, F. C. (1983). 2-Oxoacid dehydrogenase complexes of Escherichia coli: cellular amounts and patterns of synthesis. J Bacteriol 156, 81-88.
    • (1983) J Bacteriol , vol.156 , pp. 81-88
    • Smith, M.W.1    Neidhardt, F.C.2
  • 42
    • 0025328796 scopus 로고
    • Involvement of pyruvate dehydrogenase in product formation in pyruvate-limited anaerobic chemostat cultures of Enterococcus faecalis NCTC 775
    • Snoep, J. L., Teixeira de Mattos, M. J., Postma, P. W. & Neijssel, O. M. (1990). Involvement of pyruvate dehydrogenase in product formation in pyruvate-limited anaerobic chemostat cultures of Enterococcus faecalis NCTC 775. Arch Microbiol 154, 50-55.
    • (1990) Arch Microbiol , vol.154 , pp. 50-55
    • Snoep, J.L.1    De Teixeira Mattos, M.J.2    Postma, P.W.3    Neijssel, O.M.4
  • 43
    • 0027507947 scopus 로고
    • Differences in sensitivity to NADH of purified pyruvate dehydrogenase complexes of Enterococcus faecalis, Lactococcus lactis, Azotobacter vinelandii and Escherichia coli: Implications for their activity in vivo
    • Snoep, J. L., de Graef, M. R., Westphal, A. H., de Kok, A., Teixeira de Mattos, M. J. & Neijssel, O. M. (1993). Differences in sensitivity to NADH of purified pyruvate dehydrogenase complexes of Enterococcus faecalis, Lactococcus lactis, Azotobacter vinelandii and Escherichia coli: implications for their activity in vivo. FEMS Microbiol Lett 114, 279-283.
    • (1993) FEMS Microbiol Lett , vol.114 , pp. 279-283
    • Snoep, J.L.1    De Graef, M.R.2    Westphal, A.H.3    De Kok, A.4    De Teixeira Mattos, M.J.5    Neijssel, O.M.6
  • 45
    • 0021996231 scopus 로고
    • Simultaneous extraction and reverse-phase high-performance liquid chromatographic determination of adenine and pyridine nucleotides in human red blood cells
    • Stocchi, V., Cucchiarini, L., Magnani, M., Chiarantini, L., Palma, P. & Crescentini, G. (1985). Simultaneous extraction and reverse-phase high-performance liquid chromatographic determination of adenine and pyridine nucleotides in human red blood cells. Anal Biochem 146, 118-124.
    • (1985) Anal Biochem , vol.146 , pp. 118-124
    • Stocchi, V.1    Cucchiarini, L.2    Magnani, M.3    Chiarantini, L.4    Palma, P.5    Crescentini, G.6
  • 47
    • 0035039153 scopus 로고    scopus 로고
    • Engineering a homoethanol pathway in Escherichia coli: Increased glycolytic flux and levels of expression of glycolytic genes during xylose fermentation
    • Tao, H., Gonzalez, R., Martinez, A., Rodriguez, M., Ingram, L. O., Preston, J. F. & Shanmugam, K. T. (2001). Engineering a homoethanol pathway in Escherichia coli: increased glycolytic flux and levels of expression of glycolytic genes during xylose fermentation. J Bacteriol 183, 2979-2988.
    • (2001) J Bacteriol , vol.183 , pp. 2979-2988
    • Tao, H.1    Gonzalez, R.2    Martinez, A.3    Rodriguez, M.4    Ingram, L.O.5    Preston, J.F.6    Shanmugam, K.T.7
  • 48
    • 0016777894 scopus 로고
    • A mutant of Escherichia coli deficient in pyruvate formate lyase
    • Varenne, S., Casse, F., Chippaux, M. & Pascal, M. C. (1975). A mutant of Escherichia coli deficient in pyruvate formate lyase. Mol Gen Genet 141, 181-184.
    • (1975) Mol Gen Genet , vol.141 , pp. 181-184
    • Varenne, S.1    Casse, F.2    Chippaux, M.3    Pascal, M.C.4
  • 49
    • 57049188930 scopus 로고    scopus 로고
    • Engineering Escherichia coli for the efficient conversion of glycerol to ethanol and co-products
    • Yazdani, S. S. & Gonzalez, R. (2008). Engineering Escherichia coli for the efficient conversion of glycerol to ethanol and co-products. Metab Eng 10, 340-351.
    • (2008) Metab Eng , vol.10 , pp. 340-351
    • Yazdani, S.S.1    Gonzalez, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.