메뉴 건너뛰기




Volumn , Issue , 2011, Pages

EI of the phosphotransferase system of escherichia coli: Mathematical modeling approach to analysis of its kinetic properties

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

EID: 79955033088     PISSN: 16878000     EISSN: 16878019     Source Type: Journal    
DOI: 10.1155/2011/579402     Document Type: Article
Times cited : (11)

References (29)
  • 1
    • 0025338715 scopus 로고
    • The bacterial phosphoenolpyruvate: Glycose phosphotransferase system
    • Meadow N. D., Fox D. K., Roseman S., The bacterial phosphoenolpyruvate: glycose phosphotransferase system Annual Review of Biochemistry 1990 59 497 542
    • (1990) Annual Review of Biochemistry , vol.59 , pp. 497-542
    • Meadow, N.D.1    Fox, D.K.2    Roseman, S.3
  • 2
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma P. W., Lengeler J. W., Jacobson G. R., Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria Microbiological Reviews 1993 57 3 543 594 (Pubitemid 23262509)
    • (1993) Microbiological Reviews , vol.57 , Issue.3 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 3
    • 0034675992 scopus 로고    scopus 로고
    • Signal transduction between a membrane-bound transporter, PtsG, and a soluble transcription factor, Mlc of Escherichia coli
    • Lee S. J., Boos W., Bouch J. P., Plumbridge J., Signal transduction between a membrane-bound transporter, PtsG, and a soluble transcription factor, Mlc of Escherichia coli EMBO Journal 2000 19 20 5353 5361
    • (2000) EMBO Journal , vol.19 , Issue.20 , pp. 5353-5361
    • Lee, S.J.1    Boos, W.2    Bouch, J.P.3    Plumbridge, J.4
  • 4
    • 0031736727 scopus 로고    scopus 로고
    • Inducer exclusion in Escherichia coli by non-PTS substrates: The role of the PEP to pyruvate ratio in determining the phosphorylation state of enzyme IIA(Glc)
    • DOI 10.1046/j.1365-2958.1998.01053.x
    • Hogema B. M., Arents J. C., Bader R., Eijkemans K., Yoshida H., Takahashi H., Aiba H., Postma P. W., Inducer exclusion in Escherichia coli by non-PTS substrates: the role of the PEP to pyruvate ratio in determining the phosphorylation state of enzyme IIA(Glc) Molecular Microbiology 1998 30 3 487 498 (Pubitemid 28497925)
    • (1998) Molecular Microbiology , vol.30 , Issue.3 , pp. 487-498
    • Hogema, B.M.1    Arents, J.C.2    Bader, R.3    Eijkemans, K.4    Yoshida, H.5    Takahashi, H.6    Aiba, H.7    Postma, P.W.8
  • 5
    • 0018965747 scopus 로고
    • Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli. Purification to homogeneity and some properties
    • Waygood E. B., Steeves T., Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli. Purification to homogeneity and some properties Canadian Journal of Biochemistry 1980 58 1 40 48 (Pubitemid 10037947)
    • (1980) Canadian Journal of Biochemistry , vol.58 , Issue.1 , pp. 40-48
    • Waygood, E.B.1    Steeves, T.2
  • 6
    • 25444463274 scopus 로고    scopus 로고
    • Transient state kinetics of enzyme I of the phosphoenolpyruvate:glycose phosphotransferase system of Escherichia coli: Equilibrium and second-order rate constants for the phosphotransfer reactions with phosphoenolpyruvate and HPr
    • DOI 10.1021/bi0502846
    • Meadow N. D., Mattoo R. L., Savtchenko R. S., Roseman S., Transient state kinetics of enzyme I of the phosphoenolpyruvate:glycose phosphotransferase system of Escherichia coli: equilibrium and second-order rate constants for the phosphotransfer reactions with phosphoenolpyruvate and HPr Biochemistry 2005 44 38 12790 12796 (Pubitemid 41377318)
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12790-12796
    • Meadow, N.D.1    Mattoo, R.L.2    Savtchenko, R.S.3    Roseman, S.4
  • 7
    • 0029616573 scopus 로고
    • Coupling the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli
    • DOI 10.1073/pnas.92.25.11583
    • Lux R., Jahreis K., Bettenbrock K., Parkinson J. S., Lengeler J. W., Coupling the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli Proceedings of the National Academy of Sciences of the United States of America 1995 92 25 11583 11587 (Pubitemid 26014158)
    • (1995) Proceedings of the National Academy of Sciences of the United States of America , vol.92 , Issue.25 , pp. 11583-11587
    • Lux, R.1    Jahreis, K.2    Bettenbrock, K.3    Parkinson, J.S.4    Lengeler, J.W.5
  • 8
    • 0028050518 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer equilibrium by fluorescence anisotropy
    • Chauvin F., Brand L., Roseman S., Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer equilibrium by fluorescence anisotropy Journal of Biological Chemistry 1994 269 32 20263 20269
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.32 , pp. 20263-20269
    • Chauvin, F.1    Brand, L.2    Roseman, S.3
  • 9
    • 0029795442 scopus 로고    scopus 로고
    • Enzyme I: The first protein and potential regulator of the bacterial phosphoenolpyruvate: Glycose phosphotransferase system
    • DOI 10.1016/0923-2508(96)84001-0
    • Chauvin F., Brand L., Roseman S., Enzyme I: the first protein and potential regulator of the bacterial phosphoenolpyruvate: glycose phosphotransferase system Research in Microbiology 1996 147 6-7 471 479 (Pubitemid 26338125)
    • (1996) Research in Microbiology , vol.147 , Issue.6-7 , pp. 471-479
    • Chauvin, F.1    Brand, L.2    Roseman, S.3
  • 10
    • 0028147241 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer transition kinetics by fluorescence anisotropy
    • Chauvin F., Brand L., Roseman S., Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer transition kinetics by fluorescence anisotropy Journal of Biological Chemistry 1994 269 32 20270 20274
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.32 , pp. 20270-20274
    • Chauvin, F.1    Brand, L.2    Roseman, S.3
  • 11
    • 0042010137 scopus 로고    scopus 로고
    • 2+ on the conformational stability and dimerization of phosphotransferase enzyme I from Escherichia coli
    • DOI 10.1110/ps.0352103
    • Dimitrova M. N., Peterkofsky A., Ginsburg A., Opposing effects of phosphoenolpyruvate and pyruvate with Mg on the conformational stability and dimerization of phosphotransferase enzyme I from Escherichia coli Protein Science 2003 12 9 2047 2056 (Pubitemid 37022825)
    • (2003) Protein Science , vol.12 , Issue.9 , pp. 2047-2056
    • Dimitrova, M.N.1    Peterkofsky, A.2    Ginsburg, A.3
  • 12
    • 0019432277 scopus 로고
    • Escherichia coli phosphoenolpyruvate dependent phosphotransferase system: Equilibrium kinetics and mechanism of enzyme I phosphorylation
    • DOI 10.1021/bi00504a015
    • Hoving H., Lolkema J. S., Robillard G. T., Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: equilibrium kinetics and mechanism of enzyme I phosphorylation Biochemistry 1981 20 1 87 93 (Pubitemid 11144750)
    • (1981) Biochemistry , vol.20 , Issue.1 , pp. 87-93
    • Hoving, H.1    Lolkema, J.S.2    Robillard, G.T.3
  • 13
    • 33745869396 scopus 로고    scopus 로고
    • Properties of the C-terminal domain of Enzyme I of the Escherichia coli phosphotransferase system
    • DOI 10.1074/jbc.M508966200
    • Patel H. V., Vyas K. A., Mattoo R. L., Southworth M., Perler F. B., Comb D., Roseman S., Properties of the C-terminal domain of Enzyme I of the Escherichia coli phosphotransferase system Journal of Biological Chemistry 2006 281 26 17579 17587 (Pubitemid 44035557)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.26 , pp. 17579-17587
    • Patel, H.V.1    Vyas, K.A.2    Mattoo, R.L.3    Southworth, M.4    Perler, F.B.5    Comb, D.6    Roseman, S.7
  • 14
    • 33745828088 scopus 로고    scopus 로고
    • The monomer/dimer transition of enzyme I of the Escherichia coli phosphotransferase system
    • DOI 10.1074/jbc.M508965200
    • Patel H. V., Vyas K. A., Savtchenko R., Roseman S., The monomer/dimer transition of enzyme I of the Escherichia coli phosphotransferase system Journal of Biological Chemistry 2006 281 26 17570 17578 (Pubitemid 44035556)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.26 , pp. 17570-17578
    • Patel, H.V.1    Vyas, K.A.2    Savtchenko, R.3    Roseman, S.4
  • 15
    • 0019332938 scopus 로고
    • Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system. Kinetic characterization
    • Saier M. H., Schmidt M. R., Lin P., Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Kinetic characterization Journal of Biological Chemistry 1980 255 18 8579 8584
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.18 , pp. 8579-8584
    • Saier, M.H.1    Schmidt, M.R.2    Lin, P.3
  • 16
    • 0020479846 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. Isolation and characterization of enzyme I from Salmonella typhimurium
    • Weigel N., Waygood E. B., Kukuruzinska M. A., Nakazawa A., Roseman S., Sugar transport by the bacterial phosphotransferase system. Isolation and characterization of enzyme I from Salmonella typhimurium Journal of Biological Chemistry 1982 257 23 14461 14469
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.23 , pp. 14461-14469
    • Weigel, N.1    Waygood, E.B.2    Kukuruzinska, M.A.3    Nakazawa, A.4    Roseman, S.5
  • 17
    • 0020479946 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system: XIV. Phosphoryl transfer reactions catalyzed by Enzyme I of Salmonella typhimurium
    • Weigel N., Kukuruzinska M. A., Nakazawa A., Waygood E. B., Roseman S., Sugar transport by the bacterial phosphotransferase system: XIV. Phosphoryl transfer reactions catalyzed by Enzyme I of Salmonella typhimurium Journal of Biological Chemistry 1982 257 23 14477 14491
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.23 , pp. 14477-14491
    • Weigel, N.1    Kukuruzinska, M.A.2    Nakazawa, A.3    Waygood, E.B.4    Roseman, S.5
  • 18
    • 0015217204 scopus 로고
    • Sugar transport. I. Isolation of a phosphotransferase system from Escherichia coli
    • Kundig W., Roseman S., Sugar transport. I. Isolation of a phosphotransferase system from Escherichia coli Journal of Biological Chemistry 1971 246 5 1393 1406
    • (1971) Journal of Biological Chemistry , vol.246 , Issue.5 , pp. 1393-1406
    • Kundig, W.1    Roseman, S.2
  • 21
    • 85047693571 scopus 로고    scopus 로고
    • Kinetic model of imidazologlycerol-phosphate synthetase from Escherichia coli
    • DOI 10.1007/s10541-005-0002-x, 2
    • Demin O. V., Goryanin I. I., Dronov S., Lebedeva G. V., Kinetic model of imidazologlycerol-phosphate synthetase from Escherichia coli Biochemistry 2004 69 12 1324 1335 (Pubitemid 40329541)
    • (2004) Biochemistry (Moscow) , vol.69 , Issue.12 , pp. 1324-1335
    • Demin, O.V.1    Goryanin, I.I.2    Dronov, S.3    Lebedeva, G.V.4
  • 23
    • 84938447945 scopus 로고
    • Direct search solution of numerical and statistical problems
    • Hook R., Jeeves T. A., Direct search solution of numerical and statistical problems Journal of the ACM 1961 8 212 229
    • (1961) Journal of the ACM , vol.8 , pp. 212-229
    • Hook, R.1    Jeeves, T.A.2
  • 24
    • 85027186089 scopus 로고
    • Selection of the order of an autoregressive model by Akaike's information criterion
    • Shibata R., Selection of the order of an autoregressive model by Akaike's information criterion Biometrika 1976 63 1 117 126
    • (1976) Biometrika , vol.63 , Issue.1 , pp. 117-126
    • Shibata, R.1
  • 25
    • 2342588097 scopus 로고    scopus 로고
    • Modeling and experimental validation of the signal transduction via the Escherichia coli sucrose phospho transferase system
    • DOI 10.1016/j.jbiotec.2004.02.002, PII S0168165604000914
    • Sauter T., Gilles E. D., Modeling and experimental validation of the signal transduction via the Escherichia coli sucrose phospho transferase system Journal of Biotechnology 2004 110 2 181 199 (Pubitemid 38578417)
    • (2004) Journal of Biotechnology , vol.110 , Issue.2 , pp. 181-199
    • Sauter, T.1    Gilles, E.D.2
  • 26
    • 0034634571 scopus 로고    scopus 로고
    • Understanding glucose transport by the bacterial phosphoenolpyruvate: Glycose phosphotransferase system on the basis of kinetic measurements in vitro
    • Rohwer J. M., Meadow N. D., Roseman S., Westerhoff H. V., Postma P. W., Understanding glucose transport by the bacterial phosphoenolpyruvate: glycose phosphotransferase system on the basis of kinetic measurements in vitro Journal of Biological Chemistry 2000 275 45 34909 34921
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.45 , pp. 34909-34921
    • Rohwer, J.M.1    Meadow, N.D.2    Roseman, S.3    Westerhoff, H.V.4    Postma, P.W.5
  • 27
    • 24044518764 scopus 로고    scopus 로고
    • 3 under those limiting continuous cultures
    • DOI 10.1016/j.bej.2005.05.012, PII S1369703X05001865
    • Hoque M. A., Ushiyama H., Tomita M., Shimizu K., Dynamic responses of the intracellular metabolite concentrations of the wild type and pykA mutant Escherichia coli against pulse addition of glucose or NH 3 under those limiting continuous cultures Biochemical Engineering Journal 2005 26 1 38 49 (Pubitemid 41219796)
    • (2005) Biochemical Engineering Journal , vol.26 , Issue.1 , pp. 38-49
    • Hoque, Md.A.1    Ushiyama, H.2    Tomita, M.3    Shimizu, K.4
  • 28
    • 0033562562 scopus 로고    scopus 로고
    • Automated sampling device for monitoring intracellular metabolite dynamics
    • DOI 10.1006/abio.1999.4048
    • Schaefer U., Boos W., Takors R., Weuster-Botz D., Automated sampling device for monitoring intracellular metabolite dynamics Analytical Biochemistry 1999 270 1 88 96 (Pubitemid 29230724)
    • (1999) Analytical Biochemistry , vol.270 , Issue.1 , pp. 88-96
    • Schaefer, U.1    Boos, W.2    Takors, R.3    Weuster-Botz, D.4
  • 29
    • 0014216879 scopus 로고
    • Correlation between changes in metabolite concentrations and rate of ion transport following glucose addition to Escherichia coli B
    • Hempfling W. P., Hfer M., Harris E. J., Pressman B. C., Correlation between changes in metabolite concentrations and rate of ion transport following glucose addition to Escherichia coli B Biochim Biophys Acta 1967 141 2 391 400
    • (1967) Biochim Biophys Acta , vol.141 , Issue.2 , pp. 391-400
    • Hempfling, W.P.1    Hfer, M.2    Harris, E.J.3    Pressman, B.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.