Reactant stationary approximation in enzyme kinetics

Journal of Physical Chemistry A

Volumn 112, Issue 37, 2008, Pages 8654-8658

  Hanson, Sonya M ^a   Schnell, Santiago ^b,c  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^b INDIANA UNIVERSITY   (United States)

^c UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEX CONCENTRATION; DYNAMIC BEHAVIORS; ENZYME-CATALYZED REACTIONS; QUASI-STEADY STATES; REACTION PARAMETERS; SUBSTRATE CONCENTRATIONS; SUFFICIENT CONDITIONS;

CHLORINE COMPOUNDS; CONCENTRATION (PROCESS); ENZYME KINETICS; ENZYMES; FOOD ADDITIVES; SUBSTRATES;

POLYNOMIAL APPROXIMATION;

ENZYME;

ARTICLE; CHEMICAL MODEL; CHEMISTRY; COMPUTER SIMULATION; ENERGY TRANSFER; KINETICS;

COMPUTER SIMULATION; ENERGY TRANSFER; ENZYMES; KINETICS; MODELS, CHEMICAL;

EID: 53049100891     PISSN: 10895639     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp8026226     Document Type: Article

References (24)

1. Barshop, B. A.; Wrenn, R. F.; Frieden, C. Analysis of numerical methods for computer simulation of kinetic processes: Development of kinsim - a flexible, portable system. Anal. Biochem. 1983, T30, 134-145.
2. Come, G. M. Mechanistic modelling of homogeneous reactors: A numerical method. Comput. Chem. Eng. 1979, 3, 603-609.
3. Cook, P. F. Cleland, W. W. Enzyme kinetics and mechanism; Garland Science: New York, 2007.
4. Cornish-Bowden, A. Fundamentals of enzyme kinetics, 3rd ed.; Portland Press: London, 2004.
5. Fersht, A. R. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding; Freeman: New York, 1999.
6. Flach, E. H.; Schnell, S. Use and abuse of the quasi-steady-state approximation. IEE Proc. Syst. Biol. 2006, 153, 187-191.
7. Heineken, F. G.; Tsuchiya, H. M.; Aris, R. On the mathematical status of the pseudo-steady hypothesis of biochemical kinetics. Math. Biosci. 1967, 1, 95-113.
8. Laidler, K. J. Theory of the transient phase in kinetics, with special reference to enzyme systems. Can. J. Chem. 1955, 33, 1614-1624.
9. Lee, L. W.; Yin, L.; Zhu, X. M.; Ao, P. Generic enzymatic rate equation under living conditions. J. Biol. Syst. 2007, 15, 495-514.
10. Li, B.; Shen, Y.; Li, B. Quasi-Steady-State Laws in Enzyme Kinetics. J. Phys. Chem. 2008, 112, 2311-2321.
11. Michaelis, L.; Menten, M. L. Die Kinetik der Invertinwirkung. Biochem. Z. 1913, 49, 333-369.
12. Palsson, B. O. On the dynamics of the irreversible Michaelis-Menten reaction mechanism. Chem. Eng. Sci. 1987, 42, 447-458.
13. Schauer, M.; Heinrich, R. Analysis of the quasi-steady-state approximation for an enzyme one-substrate reaction. J. Theor. Biol. 1979, 79, 425-442.
14. Schnell, S.; Maini, P. K. Enzyme kinetics at high enzyme concentration. Bull. Math. Biol. 2000, 62, 483-499.
15. max estimates. Comments Theor. Biol. 2003, 8, 169-187.
16. Schnell, S.; Mendoza, C. Enzyme kinetics of multiple alternative substrates. J. Math. Chem. 2000, 27, 155-170.
17. Schnell, S.; Mendoza, C. Time-dependent closed form solutions for fully competitive enzyme reactions. Bull. Math. Biol. 2000, 62, 321-336.
18. Turányi, T.; Tomlin, A. S.; Pilling, M. J. On the error of the quasisteady state approximation. J. Phys. Chem. 1993, 97, 163-172.
19. Segel, I. H. Enzyme Kinetics: Behavior and analysis of rapid equilibrium and steady-state enzyme systems; Wiley: New York, 1975.
20. Segel, L. A. Modeling dynamic phenomena in molecular and cellular biology; Cambridge University Press: Cambridge, 1984.
21. Segel, L. A. On the validity of the steady-state assumption of enzyme kinetics. Bull. Math. Biol. 1988, 50, 579-593.
22. Segel, L. A.; Slemrod, M. The quasi-steady-state assumption: a case study in perturbation. SIAM Rev. 1989, 31, 446-477.
23. Wayne, R. P. Principles and applications of photochemistry; Oxford University Press: Oxford, 1988.
24. Zimmerle, C. T.; Frieden, C. Analysis of progress curves by simulations generated by numerical integration. Biochem. J. 1989, 258, 381-387.