1.

Record Nr.

UNINA9910298269003321

Autore

Baici Antonio

Titolo

Kinetics of Enzyme-Modifier Interactions : Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms / / by Antonio Baici

Pubbl/distr/stampa

Vienna : , : Springer Vienna : , : Imprint : Springer, , 2015

ISBN

3-7091-1402-0

Edizione

[1st ed. 2015.]

Descrizione fisica

1 online resource (503 p.)

Disciplina

570

570285

571.4

572.6

Soggetti

Enzymology

Proteins 

Bioinformatics 

Computational biology 

Biophysics

Biological physics

Protein-Ligand Interactions

Computer Appl. in Life Sciences

Biological and Medical Physics, Biophysics

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Note generali

Description based upon print version of record.

Nota di bibliografia

Includes bibliographical references at the end of each chapters and index.

Nota di contenuto

Basic Knowledge -- The General Modifier Mechanism -- Taxonomy of Enzyme-Modifier Interactions and the Specific Velocity Plot -- Complements to Enzyme-Modifier Interactions -- The Basic Mechanisms of Inhibition and Nonessential Activation -- Multiple Enzyme-Modifier Interactions -- Multiple Interactions: Essential Activation and Liberation -- Slow-Onset Enzyme Inhibition -- Enzyme Inactivation with a Note on the Significance of Slow Modification Processes.- Dichotomous Keys to Enzyme-Modification Mechanisms. .

Sommario/riassunto

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.