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Volumn 66, Issue 5, 2000, Pages 1844-1850

Metabolic analysis of Escherichia coli in the presence and absence of the carboxylating enzymes phosphoenolpyruvate carboxylase and pyruvate carboxylase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; PHOSPHOENOLPYRUVATE CARBOXYLASE; PYRUVATE CARBOXYLASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 0034019872     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.5.1844-1850.2000     Document Type: Article
Times cited : (96)

References (36)
  • 1
    • 0018393802 scopus 로고
    • Identification of metabolic model: Citrate production from glucose by Candida lipolytica
    • Aiba, S., and M. Matsuoka. 1979. Identification of metabolic model: citrate production from glucose by Candida lipolytica. Biotechnol. Bioeng. 21:1373-1386.
    • (1979) Biotechnol. Bioeng. , vol.21 , pp. 1373-1386
    • Aiba, S.1    Matsuoka, M.2
  • 2
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann, E., B. Ochs, and K.-J. Abel. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.-J.3
  • 3
    • 0029035048 scopus 로고
    • The structure and the mechanism of action of pyruvate carboxylase
    • Attwood, P. V. 1995. The structure and the mechanism of action of pyruvate carboxylase. Int. J. Biochem. Cell Biol. 27:231-249.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 231-249
    • Attwood, P.V.1
  • 5
    • 0031036839 scopus 로고    scopus 로고
    • The ldhA gene encoding the fermentative lactate dehydrogenase of Escherichia coli
    • Bunch, P. K., F. Mat-Jan, N. Lee, and D. P. Clark. 1997. The ldhA gene encoding the fermentative lactate dehydrogenase of Escherichia coli. Microbiology 143:187-195.
    • (1997) Microbiology , vol.143 , pp. 187-195
    • Bunch, P.K.1    Mat-Jan, F.2    Lee, N.3    Clark, D.P.4
  • 6
    • 0027377702 scopus 로고
    • Alteration of growth yield by overexpression of phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxykinase in Escherichia coli
    • Chao, P.-Y., and J. C. Liao. 1993. Alteration of growth yield by overexpression of phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxykinase in Escherichia coli. Appl. Environ. Microbiol. 59:4261-4265.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 4261-4265
    • Chao, P.-Y.1    Liao, J.C.2
  • 7
    • 0024723183 scopus 로고
    • The fermentation pathways of Escherichia coli
    • Clark, D. P. 1989. The fermentation pathways of Escherichia coli. FEMS Microbiol. Rev. 63:223-234.
    • (1989) FEMS Microbiol. Rev. , vol.63 , pp. 223-234
    • Clark, D.P.1
  • 8
    • 0343203935 scopus 로고
    • Influence of expression of the pet operon on intracellular metabolic fluxes of Escherichia coli
    • Diaz-Ricci, J. C., M. Tsu, and J. E. Bailey. 1992. Influence of expression of the pet operon on intracellular metabolic fluxes of Escherichia coli. Biotechnol. Bioeng. 38:1318-1324.
    • (1992) Biotechnol. Bioeng. , vol.38 , pp. 1318-1324
    • Diaz-Ricci, J.C.1    Tsu, M.2    Bailey, J.E.3
  • 9
    • 0029795574 scopus 로고    scopus 로고
    • Pyruvate carboxylase from Rhizobium etli: Mutant characterization, nucleotide sequence, and physiological role
    • Dunn, M. F., G. Encarnacion, G. Araiza, M. C. Vargas, A. Davalos, H. Peralta, Y. Mora, and J. Mora. 1996. Pyruvate carboxylase from Rhizobium etli: mutant characterization, nucleotide sequence, and physiological role. J. Bacteriol. 178:5960-5970.
    • (1996) J. Bacteriol. , vol.178 , pp. 5960-5970
    • Dunn, M.F.1    Encarnacion, G.2    Araiza, G.3    Vargas, M.C.4    Davalos, A.5    Peralta, H.6    Mora, Y.7    Mora, J.8
  • 10
    • 0031562034 scopus 로고    scopus 로고
    • Optimization of the ion-exchange analysis of organic acids from fermentation
    • Eiteman, M. A., and M. J. Chastain. 1997. Optimization of the ion-exchange analysis of organic acids from fermentation. Anal. Chim. Acta 338:69-75.
    • (1997) Anal. Chim. Acta , vol.338 , pp. 69-75
    • Eiteman, M.A.1    Chastain, M.J.2
  • 11
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacp expression vector
    • Furste, J. P., W. Pansegrau, R. Frank, H. Blocker, P. Scholz, M. Bagdagarian, and E. Landa. 1986. Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48:119-131.
    • (1986) Gene , vol.48 , pp. 119-131
    • Furste, J.P.1    Pansegrau, W.2    Frank, R.3    Blocker, H.4    Scholz, P.5    Bagdagarian, M.6    Landa, E.7
  • 12
    • 0027909872 scopus 로고
    • Analysis of metabolic fluxes in batch and continuous cultures of Bacillus subtilis
    • Goel, A., J. Ferrance, J. Jeong, and M. M. Ataai. 1993. Analysis of metabolic fluxes in batch and continuous cultures of Bacillus subtilis. Biotechnol. Bioeng. 42:686-696.
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 686-696
    • Goel, A.1    Ferrance, J.2    Jeong, J.3    Ataai, M.M.4
  • 13
    • 0031756452 scopus 로고    scopus 로고
    • Expression of pyruvate carboxylase enhances succinate production in Escherichia coli without affecting glucose uptake
    • Gokarn, R. R., M. A. Eiteman, and E. Altman. 1998. Expression of pyruvate carboxylase enhances succinate production in Escherichia coli without affecting glucose uptake. Biotechnol. Lett. 20:795-798.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 795-798
    • Gokarn, R.R.1    Eiteman, M.A.2    Altman, E.3
  • 15
    • 0016294957 scopus 로고
    • Pyruvateformate lyase of Escherichia coli: The acetyl-enzyme intermediate
    • Knappe, J., H. P. Blaschkowski, P. Grobner, and T. Schmitt. 1974. Pyruvateformate lyase of Escherichia coli: the acetyl-enzyme intermediate. Eur. J. Biochem. 50:253-263.
    • (1974) Eur. J. Biochem. , vol.50 , pp. 253-263
    • Knappe, J.1    Blaschkowski, H.P.2    Grobner, P.3    Schmitt, T.4
  • 16
    • 0013894468 scopus 로고
    • The role and control of the glyoxylate cycle in Escherichia coli
    • Kornberg, H. 1966. The role and control of the glyoxylate cycle in Escherichia coli. Biochem. J. 99:1-11.
    • (1966) Biochem. J. , vol.99 , pp. 1-11
    • Kornberg, H.1
  • 17
    • 0029814919 scopus 로고    scopus 로고
    • Role of NAD in regulating the adhe gene of Escherichia coli
    • Leonardo, M. R., Y. Dailly, and D. P. Clark. 1996. Role of NAD in regulating the adhE gene of Escherichia coli. J. Bacteriol. 178:6013-6018.
    • (1996) J. Bacteriol. , vol.178 , pp. 6013-6018
    • Leonardo, M.R.1    Dailly, Y.2    Clark, D.P.3
  • 19
    • 0020059725 scopus 로고
    • Genetic regulation of glyoxylate shunt in Escherichia coli K-12
    • Maloy, S. R., and W. D. Nunn. 1982. Genetic regulation of glyoxylate shunt in Escherichia coli K-12. J. Bacteriol. 149:173-180.
    • (1982) J. Bacteriol. , vol.149 , pp. 173-180
    • Maloy, S.R.1    Nunn, W.D.2
  • 20
    • 0029930612 scopus 로고    scopus 로고
    • Enhanced production of succinic acid by overexpression of phosphoenolpyruvate carboxylase in Escherichia coll
    • Millard, C. S., Y.-P. Chao, J. C. Liao, and M. I. Donnelly. 1996. Enhanced production of succinic acid by overexpression of phosphoenolpyruvate carboxylase in Escherichia coll. Appl. Environ. Microbiol. 62:1808-1810.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1808-1810
    • Millard, C.S.1    Chao, Y.-P.2    Liao, J.C.3    Donnelly, M.I.4
  • 21
    • 0017253676 scopus 로고
    • Some properties of the pyruvate carboxylase from Pseudomonas fluorescens
    • Milrad de Forchetti, S. R., and J. J. Cazzulo. 1976. Some properties of the pyruvate carboxylase from Pseudomonas fluorescens. J. Gen. Microbiol. 93: 75-81.
    • (1976) J. Gen. Microbiol. , vol.93 , pp. 75-81
    • Milrad De Forchetti, S.R.1    Cazzulo, J.J.2
  • 22
    • 0021918026 scopus 로고
    • Equations and calculations of product yields and preferred pathways for butanediol and mixed acid fermentations
    • Papoutsakis, E. T., and C. L. Meyer. 1985. Equations and calculations of product yields and preferred pathways for butanediol and mixed acid fermentations. Biotechnol. Bioeng. 27:56-66.
    • (1985) Biotechnol. Bioeng. , vol.27 , pp. 56-66
    • Papoutsakis, E.T.1    Meyer, C.L.2
  • 23
    • 0343196707 scopus 로고    scopus 로고
    • Metabolic and physiological studies of Corynebacterium glutamicum mutants
    • Park, S. M., A. J. Sinskey, and G. Stephanopoulos. 1997. Metabolic and physiological studies of Corynebacterium glutamicum mutants. Biotechnol. Bioeng. 55:864-879.
    • (1997) Biotechnol. Bioeng. , vol.55 , pp. 864-879
    • Park, S.M.1    Sinskey, A.J.2    Stephanopoulos, G.3
  • 24
    • 0014599987 scopus 로고
    • Pyruvate carboxylase in Rhodopseudomonas spheroides
    • Payne, J., and J. G. Morris. 1969. Pyruvate carboxylase in Rhodopseudomonas spheroides. J. Gen. Microbiol. 59:97-101.
    • (1969) J. Gen. Microbiol. , vol.59 , pp. 97-101
    • Payne, J.1    Morris, J.G.2
  • 25
    • 0031000531 scopus 로고    scopus 로고
    • Pyruvate carboxylase as an anaplerotic enzyme in Corynebacterium glutamicum
    • Peters-Wendisch, P. G., V. F. Wendisch, S. Paul, B. J. Eikmanns, and H. Sahm. 1997. Pyruvate carboxylase as an anaplerotic enzyme in Corynebacterium glutamicum. Microbiology 143:1095-1103.
    • (1997) Microbiology , vol.143 , pp. 1095-1103
    • Peters-Wendisch, P.G.1    Wendisch, V.F.2    Paul, S.3    Eikmanns, B.J.4    Sahm, H.5
  • 26
    • 0023421727 scopus 로고
    • Metabolic pathway rates and culture fluorescence in batch fermentations of Clostridium acetobutylicum
    • Reardon, K. F., T. H. Scheper, and J. E. Bailey. 1987. Metabolic pathway rates and culture fluorescence in batch fermentations of Clostridium acetobutylicum. Biotechnol. Prog. 3:153-167.
    • (1987) Biotechnol. Prog. , vol.3 , pp. 153-167
    • Reardon, K.F.1    Scheper, T.H.2    Bailey, J.E.3
  • 27
    • 0025945913 scopus 로고
    • - levels and pH on growth, succinate production, and enzyme activities of Anaerobiospirillum succiniciproducens
    • - levels and pH on growth, succinate production, and enzyme activities of Anaerobiospirillum succiniciproducens. Appl. Environ. Microbiol. 57:3013-3019.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 3013-3019
    • Samuelov, N.S.1    Lamed, R.2    Lowe, S.3    Zeikus, J.G.4
  • 28
    • 0031085246 scopus 로고    scopus 로고
    • Expression of Ascaris suum malic enzyme in a mutant Escherichia coli allows production of succinic acid from glucose
    • Stols, L., G. Kulkarni, B. G. Harris, and M. I. Donnelly. 1997. Expression of Ascaris suum malic enzyme in a mutant Escherichia coli allows production of succinic acid from glucose. Appl. Biochem. Biotechnol. 63/65:153-158.
    • (1997) Appl. Biochem. Biotechnol. , vol.63-65 , pp. 153-158
    • Stols, L.1    Kulkarni, G.2    Harris, B.G.3    Donnelly, M.I.4
  • 29
    • 0014429571 scopus 로고
    • Kinetics of Escherichia coli B d-lactate dehydrogenase and evidence for pyruvate-cuntrolled change in conformation
    • Tarmy, E. M., and N. O. Kaplan. 1968. Kinetics of Escherichia coli B d-lactate dehydrogenase and evidence for pyruvate-cuntrolled change in conformation. J. Biol. Chem. 243:2587-2596.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2587-2596
    • Tarmy, E.M.1    Kaplan, N.O.2
  • 30
    • 0014429554 scopus 로고
    • Chemical characterization of d-lactate dehydrogenase from Escherichia coli B
    • Tarmy, E. M., and N. O. Kaplan. 1968. Chemical characterization of d-lactate dehydrogenase from Escherichia coli B. J. Biol. Chem. 243:2587-2596.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2587-2596
    • Tarmy, E.M.1    Kaplan, N.O.2
  • 31
    • 0026026940 scopus 로고
    • Site directed mutagenesis of phosphoenolpyruvate carboxylase from E. coli; the role of his-579 in the catalytic and regulatory functions
    • Terada, K., T. Murata, and K. Izui. 1991. Site directed mutagenesis of phosphoenolpyruvate carboxylase from E. coli; the role of his-579 in the catalytic and regulatory functions. J. Biochem. 109:49-54.
    • (1991) J. Biochem. , vol.109 , pp. 49-54
    • Terada, K.1    Murata, T.2    Izui, K.3
  • 32
    • 0024063815 scopus 로고
    • Application of metabolic pathway stoichiometry to statistical analysis of bioreactor measurement data
    • Tsai, S. P., and Y. H. Lee. 1988. Application of metabolic pathway stoichiometry to statistical analysis of bioreactor measurement data. Biotechnol. Bioeng. 32:713-715.
    • (1988) Biotechnol. Bioeng. , vol.32 , pp. 713-715
    • Tsai, S.P.1    Lee, Y.H.2
  • 33
    • 0001985853 scopus 로고
    • Flux determination in cellular bioreaction networks. Application to lysine fermentations
    • S. Sikdar, M. Bier, and P. Todd (ed.), CRC Press, Inc., Boca Raton, Fla.
    • Vallino, J. J., and G. Stephanopoulos. 1990. Flux determination in cellular bioreaction networks. Application to lysine fermentations, p. 205-219. In S. Sikdar, M. Bier, and P. Todd (ed.), Frontiers in bioprocessing. CRC Press, Inc., Boca Raton, Fla.
    • (1990) Frontiers in Bioprocessing , pp. 205-219
    • Vallino, J.J.1    Stephanopoulos, G.2
  • 34
    • 0027572102 scopus 로고
    • Metabolic flux distributions in corynebacterium glutamicum during growth and lysine overproduction
    • Vallino, J. J., and G. Stephanopoulos. 1993. Metabolic flux distributions in Corynebacterium glutamicum during growth and lysine overproduction. Biotechnol. Bioeng. 41:633-646.
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 633-646
    • Vallino, J.J.1    Stephanopoulos, G.2
  • 35
    • 0031007854 scopus 로고    scopus 로고
    • Environmental and physiological factors affecting the succinate product ratio during carbohydrate fermentation by Actinobacillus sp. 130Z
    • Van der Werf, M. J., M. V. Guettler, M. K. Jain, and J. G. Zeikus. 1997. Environmental and physiological factors affecting the succinate product ratio during carbohydrate fermentation by Actinobacillus sp. 130Z. Arch. Microbiol. 167:332-334.
    • (1997) Arch. Microbiol. , vol.167 , pp. 332-334
    • Van Der Werf, M.J.1    Guettler, M.V.2    Jain, M.K.3    Zeikus, J.G.4
  • 36
    • 0032484705 scopus 로고    scopus 로고
    • Proposed mechanism of acetate accumulation in two recombinant Escherichia coli strains during high density fermentation
    • Van de Walle, M., and J. Shiloach. 1998. Proposed mechanism of acetate accumulation in two recombinant Escherichia coli strains during high density fermentation. Biotechnol. Bioeng. 57:71-78.
    • (1998) Biotechnol. Bioeng. , vol.57 , pp. 71-78
    • Van De Walle, M.1    Shiloach, J.2


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