메뉴 건너뛰기




Volumn 83, Issue 2, 1997, Pages 132-138

Enhancement of glucose metabolism in a pyruvic acid-hyperproducing Escherichia coli mutant defective in F1-ATPase activity

Author keywords

Escherichia coli; F1 ATPase; glycolytic pathway; phosphoglycerate kinase; phosphotransferase system; pyruvate kinase; pyruvic acid

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; CELL CULTURE; COLIFORM BACTERIA; ENZYME KINETICS; ENZYMES; GLUCOSE; GROWTH KINETICS; OXYGEN;

EID: 0030900674     PISSN: 0922338X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0922-338X(97)83571-4     Document Type: Article
Times cited : (47)

References (29)
  • 1
    • 77956937260 scopus 로고
    • Enzymes as control elements in metabolic regulation
    • Boyer, P. D. (ed.). Academic Press, New York and London
    • Atkinson, D. E.: Enzymes as control elements in metabolic regulation, p. 461-489. In Boyer, P. D. (ed.), The enzymes. Academic Press, New York and London (1970).
    • (1970) The Enzymes , pp. 461-489
    • Atkinson, D.E.1
  • 2
    • 0018185175 scopus 로고
    • Phosphofructokinases from Escherichia coli
    • Babul, J.: Phosphofructokinases from Escherichia coli. J. Biol. Chem., 253, 4350-4355 (1978).
    • (1978) J. Biol. Chem. , vol.253 , pp. 4350-4355
    • Babul, J.1
  • 3
    • 0016424514 scopus 로고
    • Regulation of the amount and of the activity of phosphofructokinases and pyruvate kinases in Escherichia coli
    • Kotlarz, D., Garreau, H., and Buc, H.: Regulation of the amount and of the activity of phosphofructokinases and pyruvate kinases in Escherichia coli. Biochim. Biophys. Acta, 381, 257-268 (1975).
    • (1975) Biochim. Biophys. Acta , vol.381 , pp. 257-268
    • Kotlarz, D.1    Garreau, H.2    Buc, H.3
  • 6
    • 0026485287 scopus 로고
    • Carbon and energy metabolism of atp mutants of Escherichia coli
    • Jensen, P. R. and Michelsen, O.: Carbon and energy metabolism of atp mutants of Escherichia coli. J. Bacteriol., 174, 7635-7641 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 7635-7641
    • Jensen, P.R.1    Michelsen, O.2
  • 8
    • 0026460088 scopus 로고
    • Stimulation of glucose catabolism in Escherichia coli by a potential futile cycle
    • Patnaik, R., Roof, W. D., Young, R. F., and Liao, J. C.: Stimulation of glucose catabolism in Escherichia coli by a potential futile cycle. J. Bacteriol., 174, 7527-7532 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 7527-7532
    • Patnaik, R.1    Roof, W.D.2    Young, R.F.3    Liao, J.C.4
  • 9
    • 0014344705 scopus 로고
    • Biochemical and genetic studies with lysine+ methionine mutants of Escherichia coli: Lipoic acid and α-ketoglutarate dehydrogenase-less mutants
    • Herbert, A. A. and Guest, J. R.: Biochemical and genetic studies with lysine+ methionine mutants of Escherichia coli: lipoic acid and α-ketoglutarate dehydrogenase-less mutants. J. Gen. Microbiol., 53, 363-381 (1968).
    • (1968) J. Gen. Microbiol. , vol.53 , pp. 363-381
    • Herbert, A.A.1    Guest, J.R.2
  • 10
    • 0015100514 scopus 로고
    • Oxidative phosphorylation in Escherichia coli K12
    • Butlin, J. D., Cox, G. B., and Gibson, F.: Oxidative phosphorylation in Escherichia coli K12. Biochem. J., 124, 75-81 (1971).
    • (1971) Biochem. J. , vol.124 , pp. 75-81
    • Butlin, J.D.1    Cox, G.B.2    Gibson, F.3
  • 11
    • 0018150070 scopus 로고
    • 1TPase of an Escherichia coli uncA mutant
    • 1TPase of an Escherichia coli uncA mutant. Biochem. Biophys. Res. Commun., 82, 596-602 (1978).
    • (1978) Biochem. Biophys. Res. Commun. , vol.82 , pp. 596-602
    • Dunn, S.D.1
  • 12
    • 0001414138 scopus 로고
    • Pyruvic acid production by lipoic acid auxotrophs of Enterobacter aerogenes
    • Yokota, A. and Takao, S,: Pyruvic acid production by lipoic acid auxotrophs of Enterobacter aerogenes. Agric. Biol. Chem., 53, 705-711 (1989).
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 705-711
    • Yokota, A.1    Takao, S.2
  • 14
    • 0018257148 scopus 로고
    • 556 in the respiratory chain of aerobically grown Escherichia coli K12
    • 556 in the respiratory chain of aerobically grown Escherichia coli K12. J. Biol. Chem., 253, 8910-8915 (1978).
    • (1978) J. Biol. Chem. , vol.253 , pp. 8910-8915
    • Kita, K.1    Yamato, I.2    Anraku, Y.3
  • 15
    • 0017124382 scopus 로고
    • The bacterial phosphoenolpyruvate: Sugar phosphotransferase system
    • Postma, P. W. and Roseman, S.: The bacterial phosphoenolpyruvate: sugar phosphotransferase system. Biochim. Biophys. Acta, 457, 213-257 (1976).
    • (1976) Biochim. Biophys. Acta , vol.457 , pp. 213-257
    • Postma, P.W.1    Roseman, S.2
  • 16
    • 0015377479 scopus 로고
    • Inducible phosphoenolpyruvate-dependent hexose phosphotransferase activities in Escherichia coli
    • Kornberg, H. L. and Reeves, R. E.: Inducible phosphoenolpyruvate-dependent hexose phosphotransferase activities in Escherichia coli. Biochem. J., 128, 1339-1344 (1972).
    • (1972) Biochem. J. , vol.128 , pp. 1339-1344
    • Kornberg, H.L.1    Reeves, R.E.2
  • 17
    • 0018831897 scopus 로고
    • Regulation of genes coding for enzyme constituents of the bacterial phosphotransferase system
    • Rephaeli, A. W. and Saier, M. H., Jr.: Regulation of genes coding for enzyme constituents of the bacterial phosphotransferase system. J. Bacteriol., 141, 658-663 (1980).
    • (1980) J. Bacteriol. , vol.141 , pp. 658-663
    • Rephaeli, A.W.1    Saier M.H., Jr.2
  • 18
    • 0016761881 scopus 로고
    • Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase
    • Curtis, S. J. and Epstein, W.: Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase. J. Bacteriol., 122, 1189-1199(1975).
    • (1975) J. Bacteriol. , vol.122 , pp. 1189-1199
    • Curtis, S.J.1    Epstein, W.2
  • 19
    • 0018407665 scopus 로고
    • Distribution of the phosphoenolpyruvate: Glucose phosphotransferase system in fermentative bacteria
    • Romano, A. H., Trifone, J. D., and Brustolon, M.: Distribution of the phosphoenolpyruvate: glucose phosphotransferase system in fermentative bacteria. J. Bacteriol., 139, 93-97 (1979).
    • (1979) J. Bacteriol. , vol.139 , pp. 93-97
    • Romano, A.H.1    Trifone, J.D.2    Brustolon, M.3
  • 20
    • 0029134725 scopus 로고
    • Partial characterization and effect of omeprazole on ATPase activity in Helicobacter pylori by using permeabilized cells
    • Belli, W. A. and Fryklund, J.: Partial characterization and effect of omeprazole on ATPase activity in Helicobacter pylori by using permeabilized cells. Antimicrob. Agents Chemother., 39, 1717-1720 (1995).
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1717-1720
    • Belli, W.A.1    Fryklund, J.2
  • 21
    • 0014082204 scopus 로고
    • Glucose and gluconate metabolism in an Escherichia coli mutant lacking phosphoglucose isomerase
    • Fraenkel, D. G. and Levisohn, S. R.: Glucose and gluconate metabolism in an Escherichia coli mutant lacking phosphoglucose isomerase. J. Bacteriol., 93, 1571-1578 (1967).
    • (1967) J. Bacteriol. , vol.93 , pp. 1571-1578
    • Fraenkel, D.G.1    Levisohn, S.R.2
  • 22
    • 0020440320 scopus 로고
    • Phosphofructokinases from Escherichia coli
    • Kotlarz, D. and Buc, H.: Phosphofructokinases from Escherichia coli. Methods Enzymol., 90, 60-70 (1982).
    • (1982) Methods Enzymol. , vol.90 , pp. 60-70
    • Kotlarz, D.1    Buc, H.2
  • 23
    • 0016416454 scopus 로고
    • Triosephosphate isomerase from yeast
    • Krietsch, W. K. G.: Triosephosphate isomerase from yeast. Methods Enzymol., 41, 434-438 (1975).
    • (1975) Methods Enzymol. , vol.41 , pp. 434-438
    • Krietsch, W.K.G.1
  • 24
    • 0016419426 scopus 로고
    • Phosphoglycerate kinase and phosphoglyceromutase from Escherichia coli
    • D'Alessio, G. and Josse, J.: Phosphoglycerate kinase and phosphoglyceromutase from Escherichia coli. Methods Enzymol., 42, 139-144 (1975).
    • (1975) Methods Enzymol. , vol.42 , pp. 139-144
    • D'Alessio, G.1    Josse, J.2
  • 25
    • 0016421634 scopus 로고
    • Enolase from Escherichia coli
    • Spring, T. G. and Wold, F.: Enolase from Escherichia coli. Methods Enzymol., 42, 323-329 (1975).
    • (1975) Methods Enzymol. , vol.42 , pp. 323-329
    • Spring, T.G.1    Wold, F.2
  • 27
    • 0016609612 scopus 로고
    • The control by respiration of the uptake of α-methyl glucoside in Escherichia coli K12
    • Hernandez-Asensio, M., Ramirez, J. M., and Del Campo, F. F.: The control by respiration of the uptake of α-methyl glucoside in Escherichia coli K12. Arch. Microbiol., 103, 155-162 (1975).
    • (1975) Arch. Microbiol. , vol.103 , pp. 155-162
    • Hernandez-Asensio, M.1    Ramirez, J.M.2    Del Campo, F.F.3
  • 28
    • 0008550672 scopus 로고
    • Control of phosphoenolpyruvate-dependent phosphotransferase-mediated sugar transport in Escherichia coli by energization of the cell membrane
    • Reider, E., Wagner, E. F., and Schweiger, M.: Control of phosphoenolpyruvate-dependent phosphotransferase-mediated sugar transport in Escherichia coli by energization of the cell membrane. Proc. Natl. Acad. Sci., USA, 76, 5529-5533 (1979).
    • (1979) Proc. Natl. Acad. Sci., USA , vol.76 , pp. 5529-5533
    • Reider, E.1    Wagner, E.F.2    Schweiger, M.3
  • 29
    • 0030021703 scopus 로고    scopus 로고
    • Changes in the cellular energy state affect the activity of the bacterial phosphotransferase system
    • Rohwer, J. M., Jensen, P. R., Shinohara, Y., Postma, P. W., and Westerhoff, H. V.: Changes in the cellular energy state affect the activity of the bacterial phosphotransferase system. Eur. J. Biochem., 235, 225-230 (1996).
    • (1996) Eur. J. Biochem. , vol.235 , pp. 225-230
    • Rohwer, J.M.1    Jensen, P.R.2    Shinohara, Y.3    Postma, P.W.4    Westerhoff, H.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.