Abstract
Any type of enzyme catalyzed reactions can be calculated from their differential equations, but steady-state equilibrium hides most intrinsic reactions. Mathematically, this problem corresponds to stiff differential equations. Empirically, initial velocities have been used to account for steady-state conditions. Competitive, noncompetitive, uncompetitive, and cooperative inhibition is calculated from initial velocities and steady-state equilibria. Substrate inhibition is calculated as progress curves from differential equations. At the end of this chapter, the reader should be able to calculate all feasible enzyme mechanisms and translate it to traditional interpretations.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Reed MC, Lieb A, Nijhout F (2010) The biological significance of substrate inhibition: a mechanism with diverse functions. Bioessays 32:422–429
Sekulic N, Konrad M, Lavie A (2007) Structural mechanism for substrate inhibition of the adenosine 5-phosphosulfate kinase domain of human 3-phosphoadenosine 5phosphosulfate synthetase 1 and its ramifications for enzyme regulation. J Biol Chem 282:22112–22121
Hofer P, Fringeli UP (1981) Acetylcholinesterase kinetics. Biophys Struct Mech 8:45–59
Brockendahl H, Müller T-M, Verfürth H (1968) Zur Kinetik der Produkthemmung. Hoppe Seyler’s Z Physiol Chem 349:21–24
Cleland WW (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products II. Inhibition nomenclature and theory. Biochim Biophys Acta 67:173–185
Berg J, Tymoczko J, Stryer L (2002) Biochemistry. W. H. Freeman and Company, New York
Dixon M, Webb EC, Thorne CJR, Tipton KF (1979) Enzymes, 3rd edn. Longman, London, p 126
Inglese J, Auld DS, Jadhav A, Johnson RL, Simeonov A, Yasgar A, Zheng W, Austin CP (2006) Quantitative high-throughput screening: a titration-based approach that efficiently identifies biological activities in large chemical libraries. Proc Natl Acad Sci USA 103:11473–11478
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
Copyright information
© 2011 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Prinz, H. (2011). Enzyme Kinetics. In: Numerical Methods for the Life Scientist. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-20820-1_7
Download citation
DOI: https://doi.org/10.1007/978-3-642-20820-1_7
Published:
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-20819-5
Online ISBN: 978-3-642-20820-1
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)