國立虎尾科技大學 |

Kinetics of Enzyme-Modifier Interactions = Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms /

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Kinetics of Enzyme-Modifier Interactions/ by Antonio Baici.
Reminder of title:	Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms /
Author:	Baici, Antonio.
Description:	XVII, 489 p. 221 illus.online resource. :
Contained By:	Springer Nature eBook
Subject:	Enzymology. -
Online resource:	https://doi.org/10.1007/978-3-7091-1402-5
ISBN:	9783709114025

Kinetics of Enzyme-Modifier Interactions = Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms /
Baici, Antonio.

Kinetics of Enzyme-Modifier InteractionsSelected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms /[electronic resource] :by Antonio Baici. - 1st ed. 2015. - XVII, 489 p. 221 illus.online resource.

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. .

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.

ISBN: 9783709114025

Standard No.: 10.1007/978-3-7091-1402-5doiSubjects--Topical Terms:

782178
Enzymology.

LC Class. No.: QD431-431.7

Dewey Class. No.: 572.6

Kinetics of Enzyme-Modifier Interactions = Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms /
LDR:04102nam a22003975i 4500 001 969849
003 DE-He213
005 20200630030455.0
007 cr nn 008mamaa
008 201211s2015 au | s |||| 0|eng d
020 $a 9783709114025 $9 978-3-7091-1402-5
024 7 $a 10.1007/978-3-7091-1402-5 $2 doi
035 $a 978-3-7091-1402-5
050 4 $a QD431-431.7
072 7 $a PSBZ $2 bicssc
072 7 $a SCI007000 $2 bisacsh
072 7 $a PSB $2 thema
082 0 4 $a 572.6 $2 23
100 1 $a Baici, Antonio. $e author. $4 aut $4 http://id.loc.gov/vocabulary/relators/aut $3 1265414
245 1 0 $a Kinetics of Enzyme-Modifier Interactions $h [electronic resource] : $b Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms / $c by Antonio Baici.
250 $a 1st ed. 2015.
264 1 $a Vienna : $b Springer Vienna : $b Imprint: Springer, $c 2015.
300 $a XVII, 489 p. 221 illus. $b online resource.
336 $a text $b txt $2 rdacontent
337 $a computer $b c $2 rdamedia
338 $a online resource $b cr $2 rdacarrier
347 $a text file $b PDF $2 rda
505 0 $a 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. .
520 $a 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.
650 0 $a Enzymology. $3 782178
650 0 $a Proteins . $3 1253493
650 0 $a Bioinformatics . $3 1253897
650 0 $a Computational biology . $3 1253898
650 0 $a Biophysics. $3 581576
650 0 $a Biological physics. $3 1253579
650 2 4 $a Protein-Ligand Interactions. $3 882815
650 2 4 $a Computer Appl. in Life Sciences. $3 593908
650 2 4 $a Biological and Medical Physics, Biophysics. $3 1113305
710 2 $a SpringerLink (Online service) $3 593884
773 0 $t Springer Nature eBook
776 0 8 $i Printed edition: $z 9783709114032
776 0 8 $i Printed edition: $z 9783709114018
776 0 8 $i Printed edition: $z 9783709119495
856 4 0 $u https://doi.org/10.1007/978-3-7091-1402-5
912 $a ZDB-2-SBL
912 $a ZDB-2-SXB
950 $a Biomedical and Life Sciences (SpringerNature-11642)
950 $a Biomedical and Life Sciences (R0) (SpringerNature-43708)