메뉴 건너뛰기




Volumn 272, Issue 8, 2005, Pages 1965-1985

The multifarious short-term regulation of ammonium assimilation of Escherichia coli: Dissection using an in silico replica

Author keywords

Ammonium assimilation; Glutamine synthetase; Robustness; Silicon cell; Systems biology

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMMONIA; CARBON; GLUTAMATE AMMONIA LIGASE; GLUTAMATE DEHYDROGENASE; GLUTAMATE SYNTHASE; GLUTAMIC ACID; GLUTAMINE; NITROGEN;

EID: 17444406291     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04626.x     Document Type: Article
Times cited : (54)

References (70)
  • 1
    • 0001258643 scopus 로고
    • On the control of gene expression
    • (Cornish-Bowden A & Cardenas ML, eds). Plenum Press, New York
    • Westerhoff HV, Koster JG, van Workum M & Rudd KE (1989) On the control of gene expression. In Control of Metabolic Processes (Cornish-Bowden A & Cardenas ML, eds), pp. 399-413. Plenum Press, New York.
    • (1989) Control of Metabolic Processes , pp. 399-413
    • Westerhoff, H.V.1    Koster, J.G.2    Van Workum, M.3    Rudd, K.E.4
  • 2
    • 0031021873 scopus 로고    scopus 로고
    • Glycolysis in bloodstream form Trypanosoma brucei can be understood in terms of the kinetics of the glycolytic enzymes
    • Bakker BM, Michels PAM, Opperdoes FR & Westerhoff HV (1997) Glycolysis in bloodstream form Trypanosoma brucei can be understood in terms of the kinetics of the glycolytic enzymes. J Biol Chem 272, 3207-3215.
    • (1997) J Biol Chem , vol.272 , pp. 3207-3215
    • Bakker, B.M.1    Michels, P.A.M.2    Opperdoes, F.R.3    Westerhoff, H.V.4
  • 4
    • 0034634571 scopus 로고    scopus 로고
    • Understanding glucose transport by the bacterial phosphoenolpyruvate: Glucose phosphotransferase system on the basis of kinetic measurements in vitro
    • Rohwer JM, Meadow ND, Roseman S, Westerhoff HV & Postma PW (2000) Understanding glucose transport by the bacterial phosphoenolpyruvate: glucose phosphotransferase system on the basis of kinetic measurements in vitro. J Biol Chem 275, 34909-34921.
    • (2000) J Biol Chem , vol.275 , pp. 34909-34921
    • Rohwer, J.M.1    Meadow, N.D.2    Roseman, S.3    Westerhoff, H.V.4    Postma, P.W.5
  • 5
    • 0033570090 scopus 로고    scopus 로고
    • Quantification of short term signaling by the epidermal growth factor receptor
    • Kholodenko BN, Demin OV, Moehren G & Hoek JB (1999) Quantification of short term signaling by the epidermal growth factor receptor. J Biol Chem 274, 30169-30181.
    • (1999) J Biol Chem , vol.274 , pp. 30169-30181
    • Kholodenko, B.N.1    Demin, O.V.2    Moehren, G.3    Hoek, J.B.4
  • 6
    • 0034877874 scopus 로고    scopus 로고
    • The silicon cell, not dead but live!
    • Westerhoff HV (2001) The silicon cell, not dead but live! Metab Eng 3, 207-210.
    • (2001) Metab Eng , vol.3 , pp. 207-210
    • Westerhoff, H.V.1
  • 8
    • 0014118692 scopus 로고
    • Regulation of glutamine synthetase. VII. Adenylyl glutamine synthetase: A new form of the enzyme with altered regulatory and kinetic properties
    • Shapiro BM, Kingdon HS & Stadtman ER (1967) Regulation of glutamine synthetase. VII. Adenylyl glutamine synthetase: a new form of the enzyme with altered regulatory and kinetic properties. Proc Natl Acad Sci USA 58, 642-649.
    • (1967) Proc Natl Acad Sci USA , vol.58 , pp. 642-649
    • Shapiro, B.M.1    Kingdon, H.S.2    Stadtman, E.R.3
  • 9
    • 0025208219 scopus 로고
    • Discovery of glutamine synthetase cascade
    • Stadtman ER (1990) Discovery of glutamine synthetase cascade. Methods Enzymol 182, 793-809.
    • (1990) Methods Enzymol , vol.182 , pp. 793-809
    • Stadtman, E.R.1
  • 12
    • 0033655445 scopus 로고    scopus 로고
    • Integration of antagonistic signals in the regulation of nitrogen assimilation in Escherichia coli
    • Ninfa AJ, Jiang P, Atkinson MR & Peliska JA (2000) Integration of antagonistic signals in the regulation of nitrogen assimilation in Escherichia coli. Curr Top Cell Regul 36, 31-75.
    • (2000) Curr Top Cell Regul , vol.36 , pp. 31-75
    • Ninfa, A.J.1    Jiang, P.2    Atkinson, M.R.3    Peliska, J.A.4
  • 14
    • 0015523879 scopus 로고
    • Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein
    • Miller RE & Stadtman ER (1972) Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein. J Biol Chem 247, 7407-7419.
    • (1972) J Biol Chem , vol.247 , pp. 7407-7419
    • Miller, R.E.1    Stadtman, E.R.2
  • 15
    • 0016697801 scopus 로고
    • Glutamate dehydrogenase from Escherichia coli: Purification and properties
    • Sakamoto N, Kotre AM & Savageau MA (1975) Glutamate dehydrogenase from Escherichia coli: purification and properties. J Bacteriol 124, 775-783.
    • (1975) J Bacteriol , vol.124 , pp. 775-783
    • Sakamoto, N.1    Kotre, A.M.2    Savageau, M.A.3
  • 16
    • 0031752273 scopus 로고    scopus 로고
    • Pathway choice in glutamate synthesis in Escherichia coli
    • Helling RB (1998) Pathway choice in glutamate synthesis in Escherichia coli. J Bacteriol 180, 4571-4575.
    • (1998) J Bacteriol , vol.180 , pp. 4571-4575
    • Helling, R.B.1
  • 17
    • 0028129875 scopus 로고
    • Why does Escherichia coli have two primary pathways for synthesis of glutamate?
    • Helling RB (1994) Why does Escherichia coli have two primary pathways for synthesis of glutamate? J Bacteriol 176, 4664-4668.
    • (1994) J Bacteriol , vol.176 , pp. 4664-4668
    • Helling, R.B.1
  • 18
    • 0025437968 scopus 로고
    • Enteric bacteria and osmotic stress: Intracellular potassium glutamate as a secondary signal of osmotic stress?
    • Booth IR & Higgins CF (1990) Enteric bacteria and osmotic stress: intracellular potassium glutamate as a secondary signal of osmotic stress? FEMS Microbiol Rev 6, 239-246.
    • (1990) FEMS Microbiol Rev , vol.6 , pp. 239-246
    • Booth, I.R.1    Higgins, C.F.2
  • 19
    • 0018236372 scopus 로고
    • Glutamate synthase: On the kinetic mechanism of the enzyme from Escherichia coli W
    • Rendina AR & Orme-Johnson WH (1978) Glutamate synthase: on the kinetic mechanism of the enzyme from Escherichia coli W. Biochemistry 17, 5388-5393.
    • (1978) Biochemistry , vol.17 , pp. 5388-5393
    • Rendina, A.R.1    Orme-Johnson, W.H.2
  • 20
    • 0014211580 scopus 로고
    • Regulation of glutamine synthetase. 3. Cumulative feedback inhibition of glutamine synthetase from Escherichia coli
    • Woolfolk CA & Stadtman ER (1967) Regulation of glutamine synthetase. 3. Cumulative feedback inhibition of glutamine synthetase from Escherichia coli. Arch Biochem Biophys 118, 736-755.
    • (1967) Arch Biochem Biophys , vol.118 , pp. 736-755
    • Woolfolk, C.A.1    Stadtman, E.R.2
  • 21
    • 0014141788 scopus 로고
    • Regulation of glutamine synthetase. 8. ATP: Glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase
    • Kingdon HS, Shapiro BM & Stadtman ER (1967) Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase. Proc Natl Acad Sci USA 58, 1703-1710.
    • (1967) Proc Natl Acad Sci USA , vol.58 , pp. 1703-1710
    • Kingdon, H.S.1    Shapiro, B.M.2    Stadtman, E.R.3
  • 22
    • 0030880188 scopus 로고    scopus 로고
    • The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction
    • Jaggi R, van Heeswijk WC, Westerhoff HV, Ollis DL & Vasudevan SG (1997) The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction. EMBO J 16, 5562-5571.
    • (1997) EMBO J , vol.16 , pp. 5562-5571
    • Jaggi, R.1    Van Heeswijk, W.C.2    Westerhoff, H.V.3    Ollis, D.L.4    Vasudevan, S.G.5
  • 23
    • 0032530281 scopus 로고    scopus 로고
    • The regulation of Escherichia coli glutamine synthetase revisited: Role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state
    • Jiang P, Peliska JA & Ninfa AJ (1998) The regulation of Escherichia coli glutamine synthetase revisited: role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state. Biochemistry 37, 12802-12810.
    • (1998) Biochemistry , vol.37 , pp. 12802-12810
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 25
    • 0032895784 scopus 로고    scopus 로고
    • Characterization of the GlnK protein of Escherichia coli
    • Atkinson MR & Ninfa AJ (1999) Characterization of the GlnK protein of Escherichia coli. Mol Microbiol 32, 301-313.
    • (1999) Mol Microbiol , vol.32 , pp. 301-313
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 26
    • 0032530304 scopus 로고    scopus 로고
    • Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Escherichia coli and its interaction with the PII protein
    • Jiang P, Peliska JA & Ninfa AJ (1998) Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Escherichia coli and its interaction with the PII protein. Biochemistry 37, 12782-12794.
    • (1998) Biochemistry , vol.37 , pp. 12782-12794
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 27
    • 0036035414 scopus 로고    scopus 로고
    • Physiological role of the GlnK signal transduction protein of Escherichia coli: Survival of nitrogen starvation
    • Blauwkamp TA & Ninfa AJ (2002) Physiological role of the GlnK signal transduction protein of Escherichia coli: survival of nitrogen starvation. Mol Microbiol 46, 203-214.
    • (2002) Mol Microbiol , vol.46 , pp. 203-214
    • Blauwkamp, T.A.1    Ninfa, A.J.2
  • 28
    • 0032530305 scopus 로고    scopus 로고
    • Reconstitution of the signal-transduction bicyclic cascade responsible for the regulation of Ntr gene transcription in Escherichia coli
    • Jiang P, Peliska JA & Ninfa AJ (1998) Reconstitution of the signal-transduction bicyclic cascade responsible for the regulation of Ntr gene transcription in Escherichia coli. Biochemistry 37, 12795-12801.
    • (1998) Biochemistry , vol.37 , pp. 12795-12801
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 29
    • 0029051027 scopus 로고
    • The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP
    • Kamberov ES, Atkinson MR & Ninfa AJ (1995) The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP. J Biol Chem 270, 17797-17807.
    • (1995) J Biol Chem , vol.270 , pp. 17797-17807
    • Kamberov, E.S.1    Atkinson, M.R.2    Ninfa, A.J.3
  • 31
    • 0016744341 scopus 로고
    • Regulation of nitrogen metabolism in Escherichia coli and Klebsiella aerogenes: Studies with the continuous-culture technique
    • Senior PJ (1975) Regulation of nitrogen metabolism in Escherichia coli and Klebsiella aerogenes: studies with the continuous-culture technique. J Bacteriol 123, 407-418.
    • (1975) J Bacteriol , vol.123 , pp. 407-418
    • Senior, P.J.1
  • 32
    • 0000060736 scopus 로고    scopus 로고
    • Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine, and D-alanine
    • (Neidhardt EA, ed.). ASM Press, Washington, D.C.
    • Reitzer LJ (1996) Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine, and D-alanine. In Escherichia coli and Salmonella: cellular and molecular biology (Neidhardt EA, ed.), pp. 391-407. ASM Press, Washington, D.C.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 391-407
    • Reitzer, L.J.1
  • 33
    • 0015147278 scopus 로고
    • The effect of carbon and nitrogen sources on the level of metabolic intermediates in Escherichia coli
    • Lowry OH, Carter J, Ward JB & Glaser L (1971) The effect of carbon and nitrogen sources on the level of metabolic intermediates in Escherichia coli. J Biol Chem 246, 6511-6521.
    • (1971) J Biol Chem , vol.246 , pp. 6511-6521
    • Lowry, O.H.1    Carter, J.2    Ward, J.B.3    Glaser, L.4
  • 34
    • 0027262505 scopus 로고
    • Nitrogen regulation in an Escherichia coli strain with a temperature sensitive glutamyl-tRNA synthetase
    • Osorio AV, Camarena L, Salazar G, Noll-Louzada M & Bastarrachea F (1993) Nitrogen regulation in an Escherichia coli strain with a temperature sensitive glutamyl-tRNA synthetase. Mol Gen Genet 239, 400-408.
    • (1993) Mol Gen Genet , vol.239 , pp. 400-408
    • Osorio, A.V.1    Camarena, L.2    Salazar, G.3    Noll-Louzada, M.4    Bastarrachea, F.5
  • 35
    • 0031882597 scopus 로고    scopus 로고
    • Perturbation of anion balance during inhibition of growth of Escherichia coli by weak acids
    • Roe AJ, McLaggan D, Davidson I, O'Byrne C & Booth IR (1998) Perturbation of anion balance during inhibition of growth of Escherichia coli by weak acids. J Bacteriol 180, 767-772.
    • (1998) J Bacteriol , vol.180 , pp. 767-772
    • Roe, A.J.1    McLaggan, D.2    Davidson, I.3    O'Byrne, C.4    Booth, I.R.5
  • 36
    • 0034749814 scopus 로고    scopus 로고
    • Roles of glutamate synthase, gltBD, and gltF in nitrogen metabolism of Escherichia coli and Klebsiella aerogenes
    • Goss TJ, Perez-Matos A & Bender RA (2001) Roles of glutamate synthase, gltBD, and gltF in nitrogen metabolism of Escherichia coli and Klebsiella aerogenes. J Bacteriol 183, 6607-6619.
    • (2001) J Bacteriol , vol.183 , pp. 6607-6619
    • Goss, T.J.1    Perez-Matos, A.2    Bender, R.A.3
  • 37
    • 0021733149 scopus 로고
    • Covalent modification of bacterial glutamine synthetase: Physiological significance
    • Kustu S, Hirschman J, Burton D, Jelesko J & Meeks JC (1984) Covalent modification of bacterial glutamine synthetase: physiological significance. Mol Gen Genet 197, 309-317.
    • (1984) Mol Gen Genet , vol.197 , pp. 309-317
    • Kustu, S.1    Hirschman, J.2    Burton, D.3    Jelesko, J.4    Meeks, J.C.5
  • 38
    • 0022295060 scopus 로고
    • Adenylylation of bacterial glutamine synthetase: Physiological significance
    • Kustu S, Hirschman J & Meeks JC (1985) Adenylylation of bacterial glutamine synthetase: physiological significance, Curr Top Cell Regul 27, 201-213.
    • (1985) Curr Top Cell Regul , vol.27 , pp. 201-213
    • Kustu, S.1    Hirschman, J.2    Meeks, J.C.3
  • 39
    • 0017871868 scopus 로고
    • Mutations that alter the covalent modification of glutamine synthetase in Salmonella typhimurium
    • Bancroft S, Rhee SG, Neumann C & Kustu S (1978) Mutations that alter the covalent modification of glutamine synthetase in Salmonella typhimurium. J Bacteriol 134, 1046-1055.
    • (1978) J Bacteriol , vol.134 , pp. 1046-1055
    • Bancroft, S.1    Rhee, S.G.2    Neumann, C.3    Kustu, S.4
  • 40
    • 0017843663 scopus 로고
    • Regulation of glutamine synthetase formation in Escherichia coli: Characterization of mutants lacking the uridylyl-transferase
    • Bloom FR, Levin MS, Poor F & Tyler B (1978) Regulation of glutamine synthetase formation in Escherichia coli: characterization of mutants lacking the uridylyl-transferase. J Bacteriol 134, 569-577.
    • (1978) J Bacteriol , vol.134 , pp. 569-577
    • Bloom, F.R.1    Levin, M.S.2    Poor, F.3    Tyler, B.4
  • 42
    • 0020687005 scopus 로고
    • Thermodynamic efficiency of microbial growth is low but optimal for maximal growth rate
    • Westerhoff HV, Hellingwerf KJ & Van Dam K (1983) Thermodynamic efficiency of microbial growth is low but optimal for maximal growth rate. Proc Natl Acad Sci USA 80, 305-309.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 305-309
    • Westerhoff, H.V.1    Hellingwerf, K.J.2    Van Dam, K.3
  • 43
    • 0026773062 scopus 로고
    • Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription
    • a Weiss V, Claverie-Martin F & Magasanik B (1992) Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription. Proc Natl Acad Sci USA 89, 5088-5092.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5088-5092
    • Weiss, V.1    Claverie-Martin, F.2    Magasanik, B.3
  • 44
    • 0015508019 scopus 로고
    • Biological function of the ammonia-induced inactivation of glutamine synthetase in Escherichia coli
    • Schutt H & Holzer H (1972) Biological function of the ammonia-induced inactivation of glutamine synthetase in Escherichia coli. Eur J Biochem 26, 68-72.
    • (1972) Eur J Biochem , vol.26 , pp. 68-72
    • Schutt, H.1    Holzer, H.2
  • 45
    • 0027281747 scopus 로고
    • The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli
    • van Heeswijk WC, Rabenberg M, Westerhoff HV & Kahn D (1993) The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli. Mol Microbiol 9, 443-457.
    • (1993) Mol Microbiol , vol.9 , pp. 443-457
    • Van Heeswijk, W.C.1    Rabenberg, M.2    Westerhoff, H.V.3    Kahn, D.4
  • 46
    • 0032499682 scopus 로고    scopus 로고
    • Ammonia acquisition in enteric bacteria: Physiological role of the ammonium/methylammonium transport B (AmtB) protein
    • Soupene E, He L, Yan D & Kustu S (1998) Ammonia acquisition in enteric bacteria: physiological role of the ammonium/methylammonium transport B (AmtB) protein. Proc Natl Acad Sci USA 95, 7030-7034.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7030-7034
    • Soupene, E.1    He, L.2    Yan, D.3    Kustu, S.4
  • 47
    • 0037133694 scopus 로고    scopus 로고
    • Ammonium/methylammonium transport (Amt) proteins facilitate diffusion of NH3 bidirectionally
    • Soupene E, Lee H & Kustu S (2002) Ammonium/methylammonium transport (Amt) proteins facilitate diffusion of NH3 bidirectionally. Proc Natl Acad Sci USA 99, 3926-3931.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3926-3931
    • Soupene, E.1    Lee, H.2    Kustu, S.3
  • 48
    • 0027369102 scopus 로고
    • Regulation of the gltBDF operon of Escherichia coli: How is a leucine-insensitive operon regulated by the leucine-responsive regulatory protein?
    • Ernsting BR, Denninger JW, Blumenthal RM & Matthews RG (1993) Regulation of the gltBDF operon of Escherichia coli: how is a leucine-insensitive operon regulated by the leucine-responsive regulatory protein? J Bacteriol 175, 7160-7169.
    • (1993) J Bacteriol , vol.175 , pp. 7160-7169
    • Ernsting, B.R.1    Denninger, J.W.2    Blumenthal, R.M.3    Matthews, R.G.4
  • 52
    • 0037022274 scopus 로고    scopus 로고
    • Product dependence and bifunctionality compromise the ultrasensitivity of signal transduction cascades
    • Ortega F, Acerenza L, Westerhoff HV, Mas F & Cascante M (2002) Product dependence and bifunctionality compromise the ultrasensitivity of signal transduction cascades. Proc Natl Acad Sci USA 99, 1170-1175.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1170-1175
    • Ortega, F.1    Acerenza, L.2    Westerhoff, H.V.3    Mas, F.4    Cascante, M.5
  • 53
  • 54
    • 0030021703 scopus 로고    scopus 로고
    • Changes in the cellular energy state affect the activity of the bacterial phosphotransferase system
    • Rohwer JM, Jensen PR, Shinohara Y, Postma PW & Westerhoff HV (1996) Changes in the cellular energy state affect the activity of the bacterial phosphotransferase system. Eur J Biochem 235, 225-230.
    • (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
  • 55
    • 0017821884 scopus 로고
    • Allosteric regulation of monocyclic interconvertible enzyme cascade systems: Use of Escherichia coli glutamine synthetase as an experimental model
    • Rhee SG, Park R, Chock PB & Stadtman ER (1978) Allosteric regulation of monocyclic interconvertible enzyme cascade systems: use of Escherichia coli glutamine synthetase as an experimental model. Proc Natl Acad Sci USA 75, 3138-3142.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3138-3142
    • Rhee, S.G.1    Park, R.2    Chock, P.B.3    Stadtman, E.R.4
  • 56
    • 0027370376 scopus 로고
    • GEPASI: A software package for modelling the dynamics, steady states and control of biochemical and other systems
    • Mendes P (1993) GEPASI: a software package for modelling the dynamics, steady states and control of biochemical and other systems. Comput Appl Biosci 9, 563-571.
    • (1993) Comput Appl Biosci , vol.9 , pp. 563-571
    • Mendes, P.1
  • 57
    • 0030921160 scopus 로고    scopus 로고
    • Biochemistry by numbers: Simulation of biochemical pathways with Gepasi 3
    • Mendes P (1997) Biochemistry by numbers: simulation of biochemical pathways with Gepasi 3. Trends Biochem Sci 22, 361-363.
    • (1997) Trends Biochem Sci , vol.22 , pp. 361-363
    • Mendes, P.1
  • 58
    • 0032406131 scopus 로고    scopus 로고
    • Non-linear optimization of biochemical pathways: Applications to metabolic engineering and parameter estimation
    • Mendes P & Kell D (1998) Non-linear optimization of biochemical pathways: applications to metabolic engineering and parameter estimation. Bioinformatics 14, 869-883.
    • (1998) Bioinformatics , vol.14 , pp. 869-883
    • Mendes, P.1    Kell, D.2
  • 59
    • 0019214015 scopus 로고
    • Kinetic mechanism of Escherichia coli glutamine synthetase
    • Meek TD & Villafranca JJ (1980) Kinetic mechanism of Escherichia coli glutamine synthetase. Biochemistry 19, 5513-5519.
    • (1980) Biochemistry , vol.19 , pp. 5513-5519
    • Meek, T.D.1    Villafranca, J.J.2
  • 60
    • 0014930781 scopus 로고
    • Some effects of adenylylation on the biosynthetic properties of the glutamine synthetase from Escherichia coli
    • Ginsburg A, Yeh J, Hennig SB & Denton MD (1970) Some effects of adenylylation on the biosynthetic properties of the glutamine synthetase from Escherichia coli. Biochemistry 9, 633-649.
    • (1970) Biochemistry , vol.9 , pp. 633-649
    • Ginsburg, A.1    Yeh, J.2    Hennig, S.B.3    Denton, M.D.4
  • 61
    • 0024653058 scopus 로고
    • Nitrogen-limited behaviour of micro-organisms growing in the presence of large concentrations of ammonium ions
    • Buurman ET, Teixeira de Mattos MJ & Neijssel OM (1989) Nitrogen-limited behaviour of micro-organisms growing in the presence of large concentrations of ammonium ions. FEMS Microbiol Lett 49, 229-232.
    • (1989) FEMS Microbiol Lett , vol.49 , pp. 229-232
    • Buurman, E.T.1    Teixeira De Mattos, M.J.2    Neijssel, O.M.3
  • 62
    • 0035920239 scopus 로고    scopus 로고
    • Molecular mechanisms of water and solute transport across archaebacterial lipid membranes
    • Mathai JC, Sprott GD & Zeidel ML (2001) Molecular mechanisms of water and solute transport across archaebacterial lipid membranes. J Biol Chem 276, 27266-27271.
    • (2001) J Biol Chem , vol.276 , pp. 27266-27271
    • Mathai, J.C.1    Sprott, G.D.2    Zeidel, M.L.3
  • 63
    • 0037973668 scopus 로고    scopus 로고
    • Why the phosphotransferase system of Escherichia coli escapes diffusion limitation
    • Francke C, Postma PW, Westerhoff HV, Blom JG & Peletier MA (2003) Why the phosphotransferase system of Escherichia coli escapes diffusion limitation. Biophys J 85, 612-622.
    • (2003) Biophys J , vol.85 , pp. 612-622
    • Francke, C.1    Postma, P.W.2    Westerhoff, H.V.3    Blom, J.G.4    Peletier, M.A.5
  • 66
    • 0003338719 scopus 로고    scopus 로고
    • Phosphorus assimilation and control of the phosphate regulon
    • (Neidhardt EA, ed.). ASM Press, Washington, D.C.
    • Wanner BL (1996) Phosphorus assimilation and control of the phosphate regulon. In Escherichia coli and Salmonella: cellular and molecular biology (Neidhardt EA, ed.), pp. 1357-1381. ASM Press, Washington, D.C.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 1357-1381
    • Wanner, B.L.1
  • 68
    • 0033968928 scopus 로고    scopus 로고
    • The glnKamtB operon. A conserved gene pair in prokaryotes
    • Thomas G, Coutts G & Merrick M (2000) The glnKamtB operon. A conserved gene pair in prokaryotes. Trends Genet 16, 11-14.
    • (2000) Trends Genet , vol.16 , pp. 11-14
    • Thomas, G.1    Coutts, G.2    Merrick, M.3
  • 69
    • 77957223611 scopus 로고
    • The continuous culture of microorganisms. 2. Construction of a chemostat
    • (Norris R & Ribbons DW, eds). Academic Press, London New York
    • Evans CGT, Herbert D & Tempest DW (1970) The continuous culture of microorganisms. 2. Construction of a chemostat. In Methods in Microbiology (Norris R & Ribbons DW, eds), pp. 277-327. Academic Press, London New York.
    • (1970) Methods in Microbiology , pp. 277-327
    • Evans, C.G.T.1    Herbert, D.2    Tempest, D.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.