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Kinetics of Enzyme-Modifier Interactions - Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms (Hardcover, 2015 ed.)
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Kinetics of Enzyme-Modifier Interactions - Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms (Hardcover, 2015 ed.)
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The kinetic mechanisms by which enzymes interact with inhibitors
and activators, collectively called modifiers, are scrutinized and
ranked taxonomically into autonomous species in a way similar to
that used in the biological classification of plants and animals.
The systematization of the mechanisms is based on two fundamental
characters: the allosteric linkage between substrate and modifier
and the factor by which a modifier affects the catalytic constant
of the enzyme. Combinations of the physically significant states of
these two characters in an ancestor-descendant-like fashion reveal
the existence of seventeen modes of interaction that cover the
needs of total, partial and fine-tuning modulation of enzyme
activity. These interactions comprise five linear and five
hyperbolic inhibition mechanisms, five nonessential activation
mechanisms and two hybrid species that manifest either hyperbolic
inhibition or nonessential activation characteristics depending on
substrate concentration. Five essential activation mechanisms,
which are taxonomically independent of the mentioned basic species,
complete the inventory of enzyme modifiers. Often masked under
conventional umbrella terms or treated as anomalous cases, all
seventeen basic inhibition and nonessential activation mechanisms
are represented in the biochemical and pharmacological literature
of this and the past century, either in the form of rapid or
slow-onset reversible interactions, or as irreversible modification
processes. The full potential of enzyme inhibitors and activators
can only be appreciated after elucidating the details of their
kinetic mechanisms of action exploring the entire range of
physiologically significant reactant concentrations. This book
highlights the wide spectrum of allosteric enzyme modification in
physiological occurrences as well as in pharmacological and
biotechnological applications that embrace simple and multiple
enzyme-modifier interactions. The reader is guided in the journey
through this still partly uncharted territory with the aid of
mechanistically-oriented criteria aimed at showing the logical way
towards the identification of a particular mechanism.
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