Abstract
This chapter provides a general introduction to the kinetics of enzyme-catalyzed reactions, with a focus on drug-metabolizing enzymes. A prerequisite to understanding enzyme kinetics is having a clear grasp of the meanings of “enzyme” and “catalysis.” Catalysts are reagents that can increase the rate of a chemical reaction without being consumed in the reaction. Enzymes are proteins that form a subset of catalysts. These concepts are further explored below.
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References
Champe PC, Harvey RA (1994) Lippincott’s Illustrated reviews: biochemistry. J. B. Lippincott Company, Philadelphia, PA
Masterson WL, Hurley CN (1989) Chemistry: principles and reactions. Saunders College Publishing, New York, NY
Lehninger AL, Nelson DL, Cox MM (1993) Principles of biochemistry. Worth Publishers, New York, NY
Stryer L (1995) Biochemistry. W. H. Freeman and Company, New York, NY
Creighton TE (1993) Proteins: structures and molecular properties. W. H. Freeman and Company, New York, NY
Obach RS (2001) The prediction of human clearance from hepatic microsomal metabolism data. Curr Opin Drug Discov Devel 4:36–44
Pelkonen O, Turpeinen M (2007) In vitro-in vivo extrapolation of hepatic clearance: biological tools, scaling factors, model assumptions and correct concentrations. Xenobiotica 37:1066–1089
Stenesh J (1993) Core topics in biochemistry. Cogno Press, Kalamazoo, MI
Segel IH (1975) Enzyme kinetics: behavior and analysis of rapid equilibrium and steady state. Wiley, Hoboken, NJ
Gabrielsson J, Weiner D (2006) Pharmacokinetic & pharmacodynamic data analysis: concepts and applications. Swedish Pharmaceutical Press, Stockholm
Nath A, Atkins WM (2006) A theoretical validation of the substrate depletion approach to determining kinetic parameters. Drug Metab Dispos 34:1433–1435
Obach RS, Reed-Hagen AE (2002) Measurement of Michaelis constants for cytochrome P450-mediated biotransformation reactions using a substrate depletion approach. Drug Metab Dispos 30:831–837
Lineweaver H, Burk D (1934) The determination of enzyme dissociation constants. J Am Chem Soc 56:658–666
Hofstee BH (1959) Non-inverted versus inverted plots in enzyme kinetics. Nature 184:1296–1298
Cornish-Bowden A (1979) Fundamentals of enzyme kinetics. Portland Press, London
Hutzler JM, Tracy TS (2002) Atypical kinetic profiles in drug metabolism reactions. Drug Metab Dispos 30:355–362
Bevington PR (1994) Data reduction and error analysis for the physical sciences. McGraw-Hill, Boston, MA
Motulsky H, Christopoulos A (2003) Fitting models to biological data using linear and nonlinear regression: a practical guide to curve fitting. GraphPad Software, Inc., San Diego, CA
Akaike H (1974) A new look at the statistical model identification. IEEE Trans Automatic Control 19:716–723
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Seibert, E., Tracy, T.S. (2014). Fundamentals of Enzyme Kinetics. In: Nagar, S., Argikar, U., Tweedie, D. (eds) Enzyme Kinetics in Drug Metabolism. Methods in Molecular Biology, vol 1113. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-758-7_2
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DOI: https://doi.org/10.1007/978-1-62703-758-7_2
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Publisher Name: Humana Press, Totowa, NJ
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