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Volumn 47, Issue 1-2, 1998, Pages 61-77

The modelling of metabolic systems. Structure, control and optimality

Author keywords

Evolutionary optimisation; Metabolic control; Metabolic systems

Indexed keywords

ADENOSINE TRIPHOSPHATE;

EID: 0031824204     PISSN: 03032647     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-2647(98)00013-6     Document Type: Article
Times cited : (76)

References (86)
  • 1
    • 0029103129 scopus 로고
    • Top-down control analysis of systems with more than one common intermediate
    • Ainscow E.K., Brand M.D. Top-down control analysis of systems with more than one common intermediate. Eur. J. Biochem. 231:1995;579-586.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 579-586
    • Ainscow, E.K.1    Brand, M.D.2
  • 2
    • 0017058392 scopus 로고
    • Evolution of enzyme function and the development of catalytic efficiency
    • Albery W.J., Knowles J.R. Evolution of enzyme function and the development of catalytic efficiency. Biochemistry. 15:1976;5631-5640.
    • (1976) Biochemistry , vol.15 , pp. 5631-5640
    • Albery, W.J.1    Knowles, J.R.2
  • 3
    • 0030574424 scopus 로고    scopus 로고
    • A possible role of adenylate metabolism in human erythrocytes. 2. Adenylate metabolism is able to improve the erythrocyte volume stabilisation
    • Ataullakhanov F.I., Komarova S.V., Martynov M.V., Vitvitsky V.M. A possible role of adenylate metabolism in human erythrocytes. 2. Adenylate metabolism is able to improve the erythrocyte volume stabilisation. J. Theor. Biol. 183:1996;307-316.
    • (1996) J. Theor. Biol. , vol.183 , pp. 307-316
    • Ataullakhanov, F.I.1    Komarova, S.V.2    Martynov, M.V.3    Vitvitsky, V.M.4
  • 4
    • 85012765723 scopus 로고
    • Limitation of metabolite concentrations and the conservation of solvent capacity in the living cell
    • Atkinson D.E. Limitation of metabolite concentrations and the conservation of solvent capacity in the living cell. Curr. Top. Cell. Regul. 1:1969;29-43.
    • (1969) Curr. Top. Cell. Regul. , vol.1 , pp. 29-43
    • Atkinson, D.E.1
  • 5
    • 0001703169 scopus 로고
    • An attempt to generalise the control coefficient concept
    • Baconnier P.F., Pachot P., Demongeot J. An attempt to generalise the control coefficient concept. J. Biol. Syst. 1:1993;335-347.
    • (1993) J. Biol. Syst. , vol.1 , pp. 335-347
    • Baconnier, P.F.1    Pachot, P.2    Demongeot, J.3
  • 6
    • 0017619243 scopus 로고
    • Evolution of enzyme catalytic power
    • Brocklehurst K. Evolution of enzyme catalytic power. Biochem. J. 163:1977;111-116.
    • (1977) Biochem. J. , vol.163 , pp. 111-116
    • Brocklehurst, K.1
  • 7
    • 0025238865 scopus 로고
    • A 'top-down' approach to the determination of control coefficients in metabolic control theory
    • Brown G.C., Hafner R.P., Brand M.D. A 'top-down' approach to the determination of control coefficients in metabolic control theory. Eur. J. Biochem. 188:1990;321-325.
    • (1990) Eur. J. Biochem. , vol.188 , pp. 321-325
    • Brown, G.C.1    Hafner, R.P.2    Brand, M.D.3
  • 8
    • 0026050621 scopus 로고
    • Total cell protein concentration as an evolutionary constraint on the metabolic control distribution in cells
    • Brown G.C. Total cell protein concentration as an evolutionary constraint on the metabolic control distribution in cells. J. Theor. Biol. 153:1991;195-203.
    • (1991) J. Theor. Biol. , vol.153 , pp. 195-203
    • Brown, G.C.1
  • 9
    • 0017287856 scopus 로고
    • The effect of natural selection on enzymic catalysis
    • Cornish-Bowden A. The effect of natural selection on enzymic catalysis. J. Mol. Biol. 101:1976;1-9.
    • (1976) J. Mol. Biol. , vol.101 , pp. 1-9
    • Cornish-Bowden, A.1
  • 10
    • 0002673180 scopus 로고
    • Metabolic control analysis in theory and practice
    • Cornish-Bowden A. Metabolic control analysis in theory and practice. Adv. Mol. Cell Biol. 11:1995;21-64.
    • (1995) Adv. Mol. Cell Biol. , vol.11 , pp. 21-64
    • Cornish-Bowden, A.1
  • 11
    • 0016811509 scopus 로고
    • Natural selection and the Michaelis constant
    • Crowley P.H. Natural selection and the Michaelis constant. J. Theor. Biol. 50:1975;461-475.
    • (1975) J. Theor. Biol. , vol.50 , pp. 461-475
    • Crowley, P.H.1
  • 12
    • 0025334686 scopus 로고
    • Integration of temporal analysis and control analysis of metabolic systems
    • Easterby J.S. Integration of temporal analysis and control analysis of metabolic systems. Biochem. J. 269:1990;255-259.
    • (1990) Biochem. J. , vol.269 , pp. 255-259
    • Easterby, J.S.1
  • 13
    • 0026802334 scopus 로고
    • Metabolic control analysis: A survey of its theoretical and experimental development
    • Fell D.A. Metabolic control analysis: a survey of its theoretical and experimental development. Biochem. J. 286:1992;313-330.
    • (1992) Biochem. J. , vol.286 , pp. 313-330
    • Fell, D.A.1
  • 14
    • 0022493181 scopus 로고
    • Fat synthesis in adipose tissue. An examination of stoichiometric constraints
    • Fell D.A., Small J.R. Fat synthesis in adipose tissue. An examination of stoichiometric constraints. Biochem. J. 238:1986;781-786.
    • (1986) Biochem. J. , vol.238 , pp. 781-786
    • Fell, D.A.1    Small, J.R.2
  • 15
    • 0023774924 scopus 로고
    • Control analysis of mammalian serine biosynthesis. Feedback inhibition on the final step
    • Fell D.A., Snell K. Control analysis of mammalian serine biosynthesis. Feedback inhibition on the final step. Biochem. J. 256:1988;97-101.
    • (1988) Biochem. J. , vol.256 , pp. 97-101
    • Fell, D.A.1    Snell, K.2
  • 16
    • 0029094167 scopus 로고
    • Physiological control of metabolic flux: The requirement for multisite modulation
    • Fell D., Thomas S. Physiological control of metabolic flux: the requirement for multisite modulation. Biochem. J. 311:1995;35-39.
    • (1995) Biochem. J. , vol.311 , pp. 35-39
    • Fell, D.1    Thomas, S.2
  • 18
    • 0016232066 scopus 로고
    • Catalysis, binding and enzyme-substrate complementarily
    • Fersht A.R. Catalysis, binding and enzyme-substrate complementarily. Proc. R. Soc. Lond. B. 187:1974;379-407.
    • (1974) Proc. R. Soc. Lond. B , vol.187 , pp. 379-407
    • Fersht, A.R.1
  • 19
    • 0025400371 scopus 로고
    • Fermentation pathway kinetics and metabolic flux control in suspended and immobilised Saccharomyces cerevisiae
    • Galazzo J., Bailey J. Fermentation pathway kinetics and metabolic flux control in suspended and immobilised Saccharomyces cerevisiae. Enzyme Microbiol. Technol. 12:1990;162-172.
    • (1990) Enzyme Microbiol. Technol. , vol.12 , pp. 162-172
    • Galazzo, J.1    Bailey, J.2
  • 21
    • 0029098807 scopus 로고
    • Concerning the measurement of flux control coefficients by enzyme titration. Steady states, quasi steady-states, and the role of time in control analytic experiments
    • Giersch C. Concerning the measurement of flux control coefficients by enzyme titration. Steady states, quasi steady-states, and the role of time in control analytic experiments. Eur. J. Biochem. 231:1995;587-592.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 587-592
    • Giersch, C.1
  • 23
    • 0025866785 scopus 로고
    • Kinetic parameters of enzymatic reactions in states of maximal activity. An evolutionary approach
    • Heinrich R., Hoffmann E. Kinetic parameters of enzymatic reactions in states of maximal activity. An evolutionary approach. J. Theor. Biol. 151:1991;249-283.
    • (1991) J. Theor. Biol. , vol.151 , pp. 249-283
    • Heinrich, R.1    Hoffmann, E.2
  • 24
    • 0015696579 scopus 로고
    • Linear theory of enzymatic chains; Its application for the analysis of the crossover theorem and of the glycolysis of human erythrocytes
    • Heinrich R., Rapoport T.A. Linear theory of enzymatic chains; its application for the analysis of the crossover theorem and of the glycolysis of human erythrocytes. Acta Biol. Med. Germ. 31:1973;479-494.
    • (1973) Acta Biol. Med. Germ. , vol.31 , pp. 479-494
    • Heinrich, R.1    Rapoport, T.A.2
  • 25
    • 0015989446 scopus 로고
    • A linear steady-state treatment of enzymatic chains. General properties, control and effector strength
    • Heinrich R., Rapoport T.A. A linear steady-state treatment of enzymatic chains. General properties, control and effector strength. Eur. J. Biochem. 42:1974;89-95.
    • (1974) Eur. J. Biochem. , vol.42 , pp. 89-95
    • Heinrich, R.1    Rapoport, T.A.2
  • 26
    • 0016529156 scopus 로고
    • Mathematical analysis of multienzyme systems II. Steady state and transient control
    • Heinrich R., Rapoport T.A. Mathematical analysis of multienzyme systems II. Steady state and transient control. BioSystems. 7:1975;130-136.
    • (1975) BioSystems , vol.7 , pp. 130-136
    • Heinrich, R.1    Rapoport, T.A.2
  • 27
    • 0025885261 scopus 로고
    • Metabolic control analysis of relaxation processes
    • Heinrich R., Reder C. Metabolic control analysis of relaxation processes. J. Theor. Biol. 151:1991;343-350.
    • (1991) J. Theor. Biol. , vol.151 , pp. 343-350
    • Heinrich, R.1    Reder, C.2
  • 29
    • 85194585993 scopus 로고    scopus 로고
    • Kinetic and thermodynamic principles determining the structural design of ATP producing systems
    • L. Luo, Q. Li, & W. Lee. Hohhot: Inner Mongolia University Press
    • Heinrich R., Stephani A. Kinetic and thermodynamic principles determining the structural design of ATP producing systems. Luo L., Li Q., Lee W. Theoretical Biophysics and Biomathematics. 1997;133-140 Inner Mongolia University Press, Hohhot.
    • (1997) Theoretical Biophysics and Biomathematics , pp. 133-140
    • Heinrich, R.1    Stephani, A.2
  • 31
    • 0023497923 scopus 로고
    • A theoretical approach to the evolution and structural design of enzymatic networks; Linear enzymatic chains, branched pathways and glycolysis of erythrocytes
    • Heinrich R., Holzhütter H.-G., Schuster S. A theoretical approach to the evolution and structural design of enzymatic networks; linear enzymatic chains, branched pathways and glycolysis of erythrocytes. Bull. Math. Biol. 49:1987;539-595.
    • (1987) Bull. Math. Biol. , vol.49 , pp. 539-595
    • Heinrich, R.1    Holzhütter, H.-G.2    Schuster, S.3
  • 32
    • 0025923478 scopus 로고
    • Mathematical analysis of enzymic reaction systems using optimization principles
    • Heinrich R., Schuster S., Holzhütter H.-G. Mathematical analysis of enzymic reaction systems using optimization principles. Eur. J. Biochem. 201:1991;1-21.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 1-21
    • Heinrich, R.1    Schuster, S.2    Holzhütter, H.-G.3
  • 33
    • 0031030714 scopus 로고    scopus 로고
    • Theoretical approaches to the evolutionary optimisation of glycolysis: Thermodynamic and kinetic constraints
    • Heinrich R., Montero F., Klipp E., Waddell T.G., Meléndez-Hevia E. Theoretical approaches to the evolutionary optimisation of glycolysis: thermodynamic and kinetic constraints. Eur. J. Biochem. 243:1997;191-201.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 191-201
    • Heinrich, R.1    Montero, F.2    Klipp, E.3    Waddell, T.G.4    Meléndez-Hevia, E.5
  • 35
    • 0027365278 scopus 로고
    • A second-order approach to metabolic control analysis
    • Höfer T., Heinrich R. A second-order approach to metabolic control analysis. J. Theor. Biol. 164:1993;85-102.
    • (1993) J. Theor. Biol. , vol.164 , pp. 85-102
    • Höfer, T.1    Heinrich, R.2
  • 38
    • 0024842144 scopus 로고
    • Metabolic dynamics in the human red cell. I. A comprehensive kinetic model
    • Joshi A., Palsson B.O. Metabolic dynamics in the human red cell. I. A comprehensive kinetic model. J. Theor. Biol. 141:1989;515-528.
    • (1989) J. Theor. Biol. , vol.141 , pp. 515-528
    • Joshi, A.1    Palsson, B.O.2
  • 39
    • 0027301842 scopus 로고
    • A universal method for achieving increases in metabolite production
    • Kacser H., Acerenza L. A universal method for achieving increases in metabolite production. Eur. J. Biochem. 216:1993;361-367.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 361-367
    • Kacser, H.1    Acerenza, L.2
  • 41
    • 0026000298 scopus 로고
    • Control theory of regulatory cascades
    • Kahn D., Westerhoff H.V. Control theory of regulatory cascades. J. Theor. Biol. 153:1991;255-285.
    • (1991) J. Theor. Biol. , vol.153 , pp. 255-285
    • Kahn, D.1    Westerhoff, H.V.2
  • 42
    • 0028566137 scopus 로고
    • Evolutionary optimisation of enzyme kinetic parameters; The effect of constraints
    • Klipp E., Heinrich R. Evolutionary optimisation of enzyme kinetic parameters; the effect of constraints. J. Theor. Biol. 171:1994;309-323.
    • (1994) J. Theor. Biol. , vol.171 , pp. 309-323
    • Klipp, E.1    Heinrich, R.2
  • 43
    • 0023610603 scopus 로고
    • On the analysis of substrate cycles in large metabolic systems
    • Leiser J., Blum J.J. On the analysis of substrate cycles in large metabolic systems. Cell Biophys. 11:1987;123-138.
    • (1987) Cell Biophys. , vol.11 , pp. 123-138
    • Leiser, J.1    Blum, J.J.2
  • 44
    • 0030571222 scopus 로고    scopus 로고
    • Pathway analysis, engineering, and physiological considerations for redirecting central metabolism
    • Liao J.C., Hou S.-Y., Chao Y.-P. Pathway analysis, engineering, and physiological considerations for redirecting central metabolism. Biotechnol. Bioeng. 52:1996;129-140.
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 129-140
    • Liao, J.C.1    Hou, S.-Y.2    Chao, Y.-P.3
  • 45
    • 0002335520 scopus 로고
    • The relationships between substrates and enzymes of glycolysis in brain
    • Lowry O.H., Passonneau J.V. The relationships between substrates and enzymes of glycolysis in brain. J. Biol. Chem. 239:1964;31-42.
    • (1964) J. Biol. Chem. , vol.239 , pp. 31-42
    • Lowry, O.H.1    Passonneau, J.V.2
  • 46
    • 0002411563 scopus 로고
    • Control of metabolic oscillations: Unpredictability, critical slowing down, optimal stability and hysteresis
    • A. Cornish-Bowden, & M.L. Cárdenas. New York: Plenum Press
    • Markus M., Hess B. Control of metabolic oscillations: unpredictability, critical slowing down, optimal stability and hysteresis. Cornish-Bowden A., Cárdenas M.L. Control of Metabolic Processes. 1990;303-313 Plenum Press, New York.
    • (1990) Control of Metabolic Processes , pp. 303-313
    • Markus, M.1    Hess, B.2
  • 47
    • 0026898402 scopus 로고
    • Synthesis of reaction mechanisms consisting of reversible and irreversible steps. 2. Formalisation and analysis of the synthesis algorithm
    • Mavrovouniotis M.L. Synthesis of reaction mechanisms consisting of reversible and irreversible steps. 2. Formalisation and analysis of the synthesis algorithm. Ind. Eng. Chem. Res. 31:1992;1637-1653.
    • (1992) Ind. Eng. Chem. Res. , vol.31 , pp. 1637-1653
    • Mavrovouniotis, M.L.1
  • 50
    • 0024280618 scopus 로고
    • Economy of design in metabolic pathways: Further remarks on the game of the pentose phosphate cycle
    • Meléndez-Hevia E., Torres N.V. Economy of design in metabolic pathways: further remarks on the game of the pentose phosphate cycle. J. Theor. Biol. 132:1988;97-111.
    • (1988) J. Theor. Biol. , vol.132 , pp. 97-111
    • Meléndez-Hevia, E.1    Torres, N.V.2
  • 52
    • 0028223931 scopus 로고
    • Optimisation of metabolism: The evolution toward simplicity through the game of the pentose phosphate cycle
    • Meléndez-Hevia E., Waddell T.G., Montero F. Optimisation of metabolism: the evolution toward simplicity through the game of the pentose phosphate cycle. J. Theor. Biol. 166:1994;201-219.
    • (1994) J. Theor. Biol. , vol.166 , pp. 201-219
    • Meléndez-Hevia, E.1    Waddell, T.G.2    Montero, F.3
  • 53
    • 0031058143 scopus 로고    scopus 로고
    • Theoretical approaches to the evolutionary optimisation of glycolysis. Chemical analysis
    • Meléndez-Hevia E., Waddell T.G., Heinrich R., Montero F. Theoretical approaches to the evolutionary optimisation of glycolysis. Chemical analysis. Eur. J. Biochem. 244:1997;527-543.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 527-543
    • Meléndez-Hevia, E.1    Waddell, T.G.2    Heinrich, R.3    Montero, F.4
  • 56
    • 0023842686 scopus 로고
    • Positive compositional algorithms in chemical reaction systems
    • Park Jr. D.J.M. Positive compositional algorithms in chemical reaction systems. Comput. Chem. 12:1988;175-188.
    • (1988) Comput. Chem. , vol.12 , pp. 175-188
    • Park D.J.M., Jr.1
  • 57
    • 0024421881 scopus 로고
    • Effect of evolution on the kinetic properties of enzymes
    • Pettersson G. Effect of evolution on the kinetic properties of enzymes. Eur. J. Biochem. 184:1989;561-566.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 561-566
    • Pettersson, G.1
  • 58
    • 0027395585 scopus 로고
    • Experimental application of top-down control analysis to metabolic systems
    • Quant P.A. Experimental application of top-down control analysis to metabolic systems. Trends Biochem. Sci. 18:1993;26-30.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 26-30
    • Quant, P.A.1
  • 59
    • 0023709196 scopus 로고
    • Metabolic control theory: A structural approach
    • Reder C. Metabolic control theory: a structural approach. J. Theor. Biol. 135:1988;175-201.
    • (1988) J. Theor. Biol. , vol.135 , pp. 175-201
    • Reder, C.1
  • 60
    • 0004267646 scopus 로고
    • Princeton, NJ: Princeton University Press
    • Rockafellar R. Convex Analysis. 1970;Princeton University Press, Princeton, NJ.
    • (1970) Convex Analysis
    • Rockafellar, R.1
  • 61
    • 0026516223 scopus 로고
    • Network analysis of intermediary metabolism using linear optimisation. I: Development of mathematical formalism
    • Savinell J.M., Palsson B.O. Network analysis of intermediary metabolism using linear optimisation. I: Development of mathematical formalism. J. Theor. Biol. 154:1992;421-454.
    • (1992) J. Theor. Biol. , vol.154 , pp. 421-454
    • Savinell, J.M.1    Palsson, B.O.2
  • 62
    • 0030574066 scopus 로고    scopus 로고
    • Control analysis in terms of generalised variables characterising metabolic systems
    • Schuster S. Control analysis in terms of generalised variables characterising metabolic systems. J. Theor. Biol. 182:1996;259-268.
    • (1996) J. Theor. Biol. , vol.182 , pp. 259-268
    • Schuster, S.1
  • 63
    • 0001112639 scopus 로고
    • Minimization of intermediate concentrations as a suggested optimality principle for biochemical networks. I. Theoretical analysis
    • Schuster S., Heinrich R. Minimization of intermediate concentrations as a suggested optimality principle for biochemical networks. I. Theoretical analysis. J. Math. Biol. 29:1991;425-442.
    • (1991) J. Math. Biol. , vol.29 , pp. 425-442
    • Schuster, S.1    Heinrich, R.2
  • 64
    • 0026802577 scopus 로고
    • The definitions of metabolic control analysis revisited
    • Schuster S., Heinrich R. The definitions of metabolic control analysis revisited. BioSystems. 27:1992;1-15.
    • (1992) BioSystems , vol.27 , pp. 1-15
    • Schuster, S.1    Heinrich, R.2
  • 65
    • 0000029295 scopus 로고
    • On elementary flux modes in biochemical reaction systems at steady state
    • Schuster S., Hilgetag C. On elementary flux modes in biochemical reaction systems at steady state. J. Biol. Syst. 2:1994;165-182.
    • (1994) J. Biol. Syst. , vol.2 , pp. 165-182
    • Schuster, S.1    Hilgetag, C.2
  • 66
    • 0009682315 scopus 로고
    • What information about the conserved-moiety structure of chemical reaction systems can be derived from their stoichiometry?
    • Schuster S., Hilgetag C. What information about the conserved-moiety structure of chemical reaction systems can be derived from their stoichiometry? J. Phys. Chem. 99:1995;8017-8023.
    • (1995) J. Phys. Chem. , vol.99 , pp. 8017-8023
    • Schuster, S.1    Hilgetag, C.2
  • 67
    • 0000068994 scopus 로고
    • Determining all extreme semi-positive conservation relations in chemical reaction systems: A test criterion for conservativity
    • Schuster S., Höfer T. Determining all extreme semi-positive conservation relations in chemical reaction systems: a test criterion for conservativity. J. Chem. Soc. Faraday Trans. 87:1991;2561-2566.
    • (1991) J. Chem. Soc. Faraday Trans. , vol.87 , pp. 2561-2566
    • Schuster, S.1    Höfer, T.2
  • 68
    • 0001125440 scopus 로고
    • Detecting strictly detailed balanced subnetworks in open chemical reaction networks
    • Schuster S., Schuster R. Detecting strictly detailed balanced subnetworks in open chemical reaction networks. J. Math. Chem. 6:1991;17-40.
    • (1991) J. Math. Chem. , vol.6 , pp. 17-40
    • Schuster, S.1    Schuster, R.2
  • 69
    • 0027537642 scopus 로고
    • Refined algorithm and computer program for calculating all non-negative fluxes admissible in steady states of biochemical reaction systems with or without some flux rates fixed
    • Schuster R., Schuster S. Refined algorithm and computer program for calculating all non-negative fluxes admissible in steady states of biochemical reaction systems with or without some flux rates fixed. CABIOS. 9:1993;79-85.
    • (1993) CABIOS , vol.9 , pp. 79-85
    • Schuster, R.1    Schuster, S.2
  • 70
    • 0027486853 scopus 로고
    • Modular analysis of the control of complex metabolic pathways
    • Schuster S., Kahn D., Westerhoff H.V. Modular analysis of the control of complex metabolic pathways. Biophys. Chem. 48:1993;1-17.
    • (1993) Biophys. Chem. , vol.48 , pp. 1-17
    • Schuster, S.1    Kahn, D.2    Westerhoff, H.V.3
  • 71
    • 0000311393 scopus 로고    scopus 로고
    • Elementary modes of functioning in biochemical networks
    • R. Cuthbertson, M. Holcombe, & R. Paton. Singapore: World Scientific
    • Schuster S., Hilgetag C., Woods J., Fell D.A. Elementary modes of functioning in biochemical networks. Cuthbertson R., Holcombe M., Paton R. Computation in Cellular and Molecular Biological Systems. 1996;151-165 World Scientific, Singapore.
    • (1996) Computation in Cellular and Molecular Biological Systems , pp. 151-165
    • Schuster, S.1    Hilgetag, C.2    Woods, J.3    Fell, D.A.4
  • 72
    • 0023995387 scopus 로고
    • MPS: An artificially intelligent software system for the analysis and synthesis of metabolic pathways
    • Seressiotis A., Bailey J.E. MPS: an artificially intelligent software system for the analysis and synthesis of metabolic pathways. Biotechnol. Bioeng. 31:1988;587-602.
    • (1988) Biotechnol. Bioeng. , vol.31 , pp. 587-602
    • Seressiotis, A.1    Bailey, J.E.2
  • 73
    • 0011984946 scopus 로고
    • Control coefficients in cellular cation homeostasis: A model analysis
    • S. Schuster, M. Rigoulet, R. Ouhabi, & J.-P. Mazat. New York: Plenum
    • Siegenbeek van Heukelom J. Control coefficients in cellular cation homeostasis: a model analysis. Schuster S., Rigoulet M., Ouhabi R., Mazat J.-P. Modern Trends in Biothermokinetics. 1993;275-279 Plenum, New York.
    • (1993) Modern Trends in Biothermokinetics , pp. 275-279
    • Siegenbeek van Heukelom, J.1
  • 74
    • 0027513359 scopus 로고
    • Responses of metabolic systems to large changes in enzyme activities and effectors. 1. The linear treatment of unbranched chains
    • Small J.R., Kacser H. Responses of metabolic systems to large changes in enzyme activities and effectors. 1. The linear treatment of unbranched chains. Eur. J. Biochem. 213:1993;613-624.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 613-624
    • Small, J.R.1    Kacser, H.2
  • 75
    • 0012981395 scopus 로고
    • Dynamic transduction of energy and internal equilibria in enzymes: A re-examination of pyruvate kinase
    • Stackhouse J., Nambiar K.P., Burbaum J.J., Stauffer D.M., Benner S.A. Dynamic transduction of energy and internal equilibria in enzymes: a re-examination of pyruvate kinase. J. Am. Chem. Soc. 107:1985;2757-2763.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2757-2763
    • Stackhouse, J.1    Nambiar, K.P.2    Burbaum, J.J.3    Stauffer, D.M.4    Benner, S.A.5
  • 76
    • 0032079021 scopus 로고    scopus 로고
    • Kinetic and thermodynamic principles determining the structural design of ATP-producing systems
    • Stephani A., Heinrich R. Kinetic and thermodynamic principles determining the structural design of ATP-producing systems. Bull. Math. Biol. 60:1998;505-543.
    • (1998) Bull. Math. Biol. , vol.60 , pp. 505-543
    • Stephani, A.1    Heinrich, R.2
  • 77
    • 0019048027 scopus 로고
    • The optimal efficiency and the economic degrees of coupling of oxidative phosphorylation
    • Stucki J.W. The optimal efficiency and the economic degrees of coupling of oxidative phosphorylation. Eur. J. Biochem. 109:1980;269-283.
    • (1980) Eur. J. Biochem. , vol.109 , pp. 269-283
    • Stucki, J.W.1
  • 78
    • 0030608156 scopus 로고
    • Control of frequency and amplitudes is shared by all enzymes in three models for yeast glycolytic oscillations
    • Teusink B., Bakker B., Westerhoff H.V. Control of frequency and amplitudes is shared by all enzymes in three models for yeast glycolytic oscillations. Biochim. Biophys. Acta. 1275:1995;204-212.
    • (1995) Biochim. Biophys. Acta , vol.1275 , pp. 204-212
    • Teusink, B.1    Bakker, B.2    Westerhoff, H.V.3
  • 79
    • 0027572102 scopus 로고
    • Metabolic flux distributions in Corynebacterium glutamicum during growth and lysine overproduction
    • Vallino J.J., Stephanopoulos G. Metabolic flux distributions in Corynebacterium glutamicum during growth and lysine overproduction. Biotechnol. Bioeng. 41:1993;633-646.
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 633-646
    • Vallino, J.J.1    Stephanopoulos, G.2
  • 80
    • 0029635981 scopus 로고
    • Parametric sensitivity of stoichiometric flux balance models applied to wild-type Escherichia coli metabolism
    • Varma A., Palsson B.O. Parametric sensitivity of stoichiometric flux balance models applied to wild-type Escherichia coli metabolism. Biotechn. Bioeng. 45:1995;69-79.
    • (1995) Biotechn. Bioeng. , vol.45 , pp. 69-79
    • Varma, A.1    Palsson, B.O.2
  • 81
    • 0013770186 scopus 로고
    • A note on the kinetics of multi-enzyme systems
    • Waley S.G. A note on the kinetics of multi-enzyme systems. Biochem. J. 91:1964;514-517.
    • (1964) Biochem. J. , vol.91 , pp. 514-517
    • Waley, S.G.1
  • 82
    • 0021908533 scopus 로고
    • A kinetic model for the interaction of energy metabolism and osmotic states of human erythrocytes. Analysis of the stationary 'in vivo' state and of time dependent variations under blood preservation conditions
    • Werner A., Heinrich R. A kinetic model for the interaction of energy metabolism and osmotic states of human erythrocytes. Analysis of the stationary 'in vivo' state and of time dependent variations under blood preservation conditions. Biomed. Biochim. Acta. 44:1985;185-212.
    • (1985) Biomed. Biochim. Acta , vol.44 , pp. 185-212
    • Werner, A.1    Heinrich, R.2
  • 83
    • 0021278674 scopus 로고
    • How do enzyme activities control metabolite concentrations? An additional theorem in the theory of metabolic control
    • Westerhoff H.V., Chen Y.-D. How do enzyme activities control metabolite concentrations? An additional theorem in the theory of metabolic control. Eur. J. Biochem. 142:1984;425-430.
    • (1984) Eur. J. Biochem. , vol.142 , pp. 425-430
    • Westerhoff, H.V.1    Chen, Y.-D.2
  • 85
    • 0011927839 scopus 로고
    • The thermodynamic basis for the partial control of oxidative phosphorylation by the adenine nucleotide translocator
    • Westerhoff V.A., Groen A.K., Wanders R.J.A. The thermodynamic basis for the partial control of oxidative phosphorylation by the adenine nucleotide translocator. Biochem. Soc. Trans. 11:1983;90-91.
    • (1983) Biochem. Soc. Trans. , vol.11 , pp. 90-91
    • Westerhoff, V.A.1    Groen, A.K.2    Wanders, R.J.A.3
  • 86
    • 0028003497 scopus 로고
    • An evolutionary approach to enzyme kinetics: Optimization of ordered mechanisms
    • Wilhelm T., Hoffmann-Klipp E., Heinrich R. An evolutionary approach to enzyme kinetics: optimization of ordered mechanisms. Bull. Math. Biol. 56:1994;65-106.
    • (1994) Bull. Math. Biol. , vol.56 , pp. 65-106
    • Wilhelm, T.1    Hoffmann-Klipp, E.2    Heinrich, R.3


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