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Quantitative Enzymology

[ Vol. 11 , Issue. 1 ]

Author(s):

David J. Timson   Pages 12 - 31 ( 20 )

Abstract:


Accurate measurement of the quantitative aspects of enzyme-catalysed reactions is critical for a deeper understanding of their mechanisms, for their exploitation in biotechnology and for targeting enzymes by drug-like molecules. It is important to move beyond basic enzyme kinetics as encapsulated in the Michaelis-Menten equation. The type and magnitude of inhibition should be determined. Since the majority of enzyme-catalysed reactions involve more than one substrate, it is critical to understand how to treat these reactions quantitatively and how their kinetic behaviour depends on the type of mechanism occurring. Some reactions do not conform to “standard” Michaelis-Menten treatment and exhibit phenomena such as cooperativity. Again it is important to put these phenomena onto a quantitative basis. Similarly the treatment of the effects of pH on enzymes is often vague and uninformative without a proper quantitative treatment. This review brings together tools and approaches for dealing with enzymes quantitatively together with original references for these approaches.

Keywords:

Enzymes, cooperativity, Michaelis-Menten equation, multisubstrate, quantitative enzymology enzyme inhibition.

Affiliation:

School of Biological Sciences, Queen’s University Belfast, Medical Biology Centre, 97 Lisburn Road, Belfast, BT9 7BL. UK.

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