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
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