Kinetic and thermodynamic principles determining the structural design of ATP-producing systems

Bulletin of Mathematical Biology

Volumn 60, Issue 3, 1998, Pages 505-543

  Stephani, Amadeus ^a   Heinrich, Reinhart ^a  

^a HUMBOLDT UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE;

BIOLOGICAL MODEL; BIOSYNTHESIS; COMPUTER SIMULATION; DEPHOSPHORYLATION; GLYCOLYSIS; KINETICS; MATHEMATICS; METABOLISM; MOLECULAR DYNAMICS; PHOSPHORYLATION; REVIEW; STOICHIOMETRY; THERMODYNAMICS;

EID: 0032079021     PISSN: 00928240     EISSN: None     Source Type: Journal    
DOI: 10.1006/bulm.1997.0028     Document Type: Article

References (37)

1. Albery, W. J. and J. R. Knowles (1976). Evolution of enzyme function and the development of catalytic efficiency. Biochem. 15, 5631-5639.
2. Cornish-Bowden, A. (1976). The effect of natural selection on enzymic catalysis. J. Mol. Biol. 101, 1-9.
3. Cornish-Bowden, A. (1981). Thermodynamic aspects of glycolysis. Biochem. Educ. 9, 133-137.
4. Crowley, P. H. (1975). Natural selection and the Michaelis constant. J. Theor. Biol. 50, 461-475.
5. Eigen, M. and G. G. Hammes (1963). Elementary steps in enzyme reactions. Adv. Enzymol. 25, 1-38.
6. Fell, D. A. and S. Thomas (1995). Physiological control of metabolic flux: the requirement for multisite modulation. Biochem. J. 311, 35-39.
7. Fersht, D. A. (1974). Catalysis, binding and enzyme-substrate complementarity. Proc. R. Soc. 187, 397-407.
8. Fersht, A. R. (1985). Enzyme Structure and Mechanism, New York: Freeman.
9. Garfinkel, D. and B. Hess (1964). Metabolic control mechanisms. VII. A detailed computer model of the glycolytic pathway in ascites cells. J. Biol. Chem. 239, 971-983.
10. Heinrich, R. and E. Hoffmann (1991). Kinetic parameters of enzymatic reactions in states of maximal activity; an evolutionary approach. J. Theor. Biol. 151, 249-283.
11. Heinrich, R., H.-G. Holzhütter and S. Schuster (1987). 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, 539-595.
12. Heinrich, R. and E. Klipp (1996). Control analysis of unbranched enzymatic chains in states of maximal activity. J. Theor. Biol. 182, 243-252.
13. Heinrich, R., F. Montero, E. Klipp, T. G. Waddell and E. Meléndez-Hevia (1997). Theoretical approaches to the evolutionary optimization of glycolysis; thermodynamic and kinetic constraints. Eur. J. Biochem. 243, 191-201.
14. Heinrich, R. and S. Schuster (1996). The Regulation of Cellular Systems, Chapman & Hall: New York.
15. Heinrich, R., S. Schuster and H.-G. Holzhütter (1991). Mathematical analysis of enzymic reaction systems using optimization principles (review). Eur. J. Biochem. 201, 1-21.
16. Hofmeyr, J.-H. S. and A. Cornish-Bowden (1991). Quantitative assessment of regulation in metabolic systems. Eur. J. Biochem. 200, 223-236.
17. Hofmeyr, J.-H. S., A. Cornish-Bowden and J. M. Rohwer (1993). Taking enzyme kinetics out of control. Putting control into regulation. Eur. J. Biochem. 212, 833-837.
18. Joshi, A and B. O. Palsson (1989). Metabolic dynamics in the human red cell. A comprehensive kinetic model (I, II). J. Theor. Biol. 141, 515-545.
19. Joshi, A. and B. O. Palsson (1990). Metabolic dynamics in the human red cell. Metabolic reaction rates (III, IV). J. Theor. Biol. 142, 41-85.
20. Kedem, O. and S. R. Caplan (1965). Degree of coupling and its relation to efficiency of energy conservation. Trans. Faraday Soc. 61, 1897-1911.
21. Kuby, S. A. (1991). A Study of Enzymes, Vol. I, Enzyme Catalysis, Kinetics and Substrate Binding, Boston: CRC Press.
22. Lehninger, A. L., D. L. Nelson and M. M. Cox (1993). Principles of Biochemistry, New York: Worth Publishers Inc.
23. Liao, J. C. and E. N. Lightfoot, Jr. (1987). Extending the quasi-steady state concept to analysis of metabolic networks. J. Theor. Biol. 126, 253-273.
24. Mavrovouniotis, M. L., G. Stephanopoulos and G. Stephanopoulos (1990). Estimation of upper bounds for the rates of enzymatic reactions. Chem. Eng. Commun. 93, 211-236.
25. Meléndez-Hevia, E. (1990). The game of the pentose phosphate cycle: a mathematical approach to study the optimization in design of metabolic pathways during evolution. Biomed. Biochim. Acta 49, 903-916.
26. Meléndez-Hevia, E. and N. V. Torres (1988). Economy of design in metabolic pathways: further remarks on the game of the pentose phosphate cycle. J. Theor. Biol. 132, 97-111.
27. Meléndez-Hevia, E., T. G. Waddel, R. Heinrich and F. Montero (1997). Theoretical approaches to the evolutionary optimization of glycolysis; chemical analysis. Eur. J. Biochem. 244, 527-543.
28. Pettersson, G. (1992). Evolutionary optimization of the catalytic efficiency of enzymes. Eur. J. Biochem. 206, 289-295.
29. Pettersson, G. (1996). A new approach for determination of the selectively favoured kinetic design of enzyme reactions. J. Theor. Biol. 183, 179-183.
30. Rapoport, T. A., R. R. Heinrich and S. M. Rapoport (1976). The regulatory principles of glycolysis in erythrocytes in vivo and in vitro. A minimal comprehensive model describing steady states, quasi-steady states and time dependent processes. Biochem. J. 154, 449-469.
31. Schuster, R., H. G. Holzhütter and G. Jacobasch (1988). Interrelations between glycolysis and the hexose monophosphate shunt in erythrocytes as studied on the basis of a mathematical model. BioSystems 22, 19-36.
32. Stryer, L. (1996). Biochemistry, 4th edn, New York: W. H. Freemann and Co.
33. Stucki, J. W. (1991). Non-equilibrium thermodynamic sensitivity of oxidative phosphorylation. Proc. R. Soc. Lond. B244, 197-202.
34. Veech, R. L. and D. A. Fell (1996). Distributed control of metabolic flux. Cell Biochemistry and Function 14, 229-236.
35. Waley, S. G. (1964). A note on the kinetics of multi-enzyme systems. Biochem. J. 91, 514-517.
36. Werner, A. and R. Heinrich (1985). 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, 185-212.
37. Willhelm, T., E. Hoffmann-Klipp, R. Heinrich (1994). An evolutionary approach to enzyme kinetics; optimization of ordered mechanisms. Bull. Math. Biol. 46, 65-106.