LEADER 05314nam 22007335 450 001 9910298269003321 005 20200630030455.0 010 $a3-7091-1402-0 024 7 $a10.1007/978-3-7091-1402-5 035 $a(CKB)3710000000436718 035 $a(EBL)2093654 035 $a(SSID)ssj0001524968 035 $a(PQKBManifestationID)11826336 035 $a(PQKBTitleCode)TC0001524968 035 $a(PQKBWorkID)11496559 035 $a(PQKB)10269089 035 $a(DE-He213)978-3-7091-1402-5 035 $a(MiAaPQ)EBC2093654 035 $a(PPN)186394136 035 $a(EXLCZ)993710000000436718 100 $a20150624d2015 u| 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 10$aKinetics of Enzyme-Modifier Interactions $eSelected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms /$fby Antonio Baici 205 $a1st ed. 2015. 210 1$aVienna :$cSpringer Vienna :$cImprint: Springer,$d2015. 215 $a1 online resource (503 p.) 300 $aDescription based upon print version of record. 311 $a3-7091-1401-2 320 $aIncludes bibliographical references at the end of each chapters and index. 327 $aBasic 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. . 330 $aThe 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. 606 $aEnzymology 606 $aProteins  606 $aBioinformatics  606 $aComputational biology  606 $aBiophysics 606 $aBiological physics 606 $aEnzymology$3https://scigraph.springernature.com/ontologies/product-market-codes/L14070 606 $aProtein-Ligand Interactions$3https://scigraph.springernature.com/ontologies/product-market-codes/L14060 606 $aComputer Appl. in Life Sciences$3https://scigraph.springernature.com/ontologies/product-market-codes/L17004 606 $aBiological and Medical Physics, Biophysics$3https://scigraph.springernature.com/ontologies/product-market-codes/P27008 615 0$aEnzymology. 615 0$aProteins . 615 0$aBioinformatics . 615 0$aComputational biology . 615 0$aBiophysics. 615 0$aBiological physics. 615 14$aEnzymology. 615 24$aProtein-Ligand Interactions. 615 24$aComputer Appl. in Life Sciences. 615 24$aBiological and Medical Physics, Biophysics. 676 $a570 676 $a570285 676 $a571.4 676 $a572.6 700 $aBaici$b Antonio$4aut$4http://id.loc.gov/vocabulary/relators/aut$01064848 906 $aBOOK 912 $a9910298269003321 996 $aKinetics of Enzyme-Modifier Interactions$92541192 997 $aUNINA