About and beyond the henri-michaelis-menten rate equation for single-substrate enzyme kinetics

Biochemical and Biophysical Research Communications

Volumn 417, Issue 3, 2012, Pages 982-985

  Bajzer, Željko ^a   Strehler, Emanuel E ^a  

^a MAYO GRADUATE SCHOOL   (United States)

Author keywords

Enzyme excess; Enzyme kinetics; Michaelis Menten rate equation; Quasi steady state; Substrate excess

Indexed keywords

ENZYME;

ARTICLE; CONCENTRATION (PARAMETERS); ENZYME KINETICS; ENZYME SUBSTRATE; MATHEMATICAL MODEL; MICHAELIS MENTEN KINETICS; PRIORITY JOURNAL; PROTEIN EXPRESSION; SIMULATION; STEADY STATE;

COMPUTER SIMULATION; ENZYMES; KINETICS; MODELS, CHEMICAL; SUBSTRATE SPECIFICITY;

EID: 84855998054     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.12.051     Document Type: Article

References (20)

1. Henri V. Théorie générale de l'action de quelques diastases. Comptes Rendus l'Académie des Sci. 1902, 135:916-919.
2. Michaelis L., Menten M.L. Die Kinetik der Invertin-Wirkung. Biochem. Z. 1913, 49:333-369.
3. Nelson D.L., Cox M.M. Lehninger Principles of Biochemistry 2008, Worth Publishers, New York. fifth ed.
4. Voet D., Voet J.G. Biochemistry 2004, Wiley, New York. third ed.
5. Buxbaum E. Fundamentals of Protein Structure and Function 2007, Springer, New York.
6. Bergethon P.R. The Physical Basis of Biochemistry 1998, Springer, New York.
7. Garret R., Grisham C.M. Biochemistry 2010, Brooks/Cole, Boston. fourth ed.
8. Segel I.H. Enzyme Kinetics 1993, Wiley, New York.
9. Schulz A.R. Enzyme Kinetics 1994, Cambridge Univ. Press.
10. Murray J.D. Mathematical Biology 2002, Springer, New York. third ed.
11. Britton N.F. Essential Mathematical Biology 2003, Springer, London.
12. Klipp E., Herwig R., Kowald A., Wierling C., Lehrach H. Systems Biology in Practice 2005, Wiley-VCH, Weinheim.
13. Kargi F. Generalized rate equation for single-substrate enzyme catalyzed reactions. Biochem. Biophys. Res. Comm. 2009, 382:57-159.
14. Segel L.A. On the validity of the steady state assumption of enzyme kinetics. Bull. Math. Biol. 1988, 50:579-593.
15. Schnell S., Mendoza C. Closed form solution for time-dependent enzyme kinetics. J. Theor. Biol. 1997, 187:207-212.
16. Schnell S., Maini P.K. Enzyme kinetics at high enzyme concentration. Bull. Math. Biol. 2000, 62:483-499.
17. Tzafriri A.R. Michaelis-Menten kinetics at high enzyme concentrations. Bull. Math. Biol. 2003, 65:1111-1129.
18. Bispo J.A.C., Bonafe C.F.S., de Souza V.B., de Almeida e Silva J.B. Extending the kinetic solution of the classic Michaelis-Menten model of enzyme action. J. Math. Chem. 2011, 49:1976-1995.
19. Li B., Li B., Shen Y. An improved method to measure all rate constants in the simplest enzyme kinetics model. J. Math. Chem. 2011, doi:10.1007/s10910-011-9922-4.
20. Bersani A.M., Dell'Acqua G. Asymptotic expansions in enzyme reactions with high enzyme concentrations. Math. Methods Appl. Sci. 2011, (doi:10.1002/mma.1495).