Chapter 14. Putting Kinetic Principles into Practice

  1. Alejandro G. Marangoni
  1. Kirk L. Parkin

Published Online: 13 MAR 2003

DOI: 10.1002/0471267295.ch14

Enzyme Kinetics: A Modern Approach

Enzyme Kinetics: A Modern Approach

How to Cite

Parkin, K. L. (2002) Putting Kinetic Principles into Practice, in Enzyme Kinetics: A Modern Approach (ed A. G. Marangoni), John Wiley & Sons, Inc., Hoboken, NJ, USA. doi: 10.1002/0471267295.ch14

Editor Information

  1. Department of Food Science, University of Guelph, Canada

Author Information

  1. Department of Food Science, Babcock Hall, University of Wisconsin, Madison, WI 53706, USA

Publication History

  1. Published Online: 13 MAR 2003
  2. Published Print: 1 NOV 2002

ISBN Information

Print ISBN: 9780471159858

Online ISBN: 9780471267294

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Keywords:

  • linear rates;
  • hyperbolic kinetics;
  • S/Km range;
  • selectivity constant;
  • substrate inhibition

Summary

The characterization of enzyme action requires the accurate and careful assessment of kinetic constants, most often as Vmax and Km. In evaluating original experimental data, or those reported in the literature, several conditions must be met to ensure proper kinetic characterization. In this chapter, simple kinetic principles are applied to illustrate and guide the evaluation and interpretation of enzyme kinetic behavior. In this context, examples will be used to illustrate some common shortcomings and flaws in the routine reporting of enzyme kinetic properties.