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Beta-Lactamases. Editors, Jean-Marie Frre

Autor Jean-Marie Frre
en Limba Engleză Hardback – 14 oct 2012
The activity of a bacterial enzyme "able to degrade penicillin" had first been described in 1940, even before the exact structure of penicillin was elucidated and, by 1970, several enzymes had been purified to homogeneity, the amino acid sequence of a staphylococcal penicillinase was also known and that of its Bacillus licheniformis counterpart was well under way. By contrast, their catalytic mechanism remained quite mysterious. A Zn++ metallo-beta-lactamase (ß-lactamase II, BcII or ßII) had also been described as soon as 1967 and later purified. It was thus surprising that the first mechanistic information demonstrating the presence of a penicillin-binding serine residue was obtained with a penicillin-sensitive DD-peptidase rather than a ß-lactamase. This seemed to open the floodgates and several class A ß-lactamases were then rapidly shown to be active-site serine enzymes. This book presents current research in the study of beta-lactamases.
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Specificații

ISBN-13: 9781613246382
ISBN-10: 1613246382
Pagini: 537
Dimensiuni: 183 x 259 x 38 mm
Greutate: 1.32 kg
Ediția:New.
Editura: NOVA SCIENCE PUB INC

Cuprins

Foreword; Before our time: early ß-lactamase papers & the people who wrote them; Structures of class A ß-lactamases; X-ray structures & mechanisms of metallo-ß-lactamases; Structures of class C ß-lactamases & perspectives in drug design; Structures of class D ß-lactamases; Kinetics of ß-lactamases in theory & practice; The mechanisms of catalysis by ß-lactamases; Insights into the mechanisms of ß-lactamases from Nuclear Magnetic Resonance studies; ß-lactams as inhibitors of ß-lactamases; Non ß-lactam inhibitors of ß-lactamases; ß-lactamase inhibitory proteins; Quantum chemistry applied to the study of ß-lactamases; Emergence of completely new sequences; Emergence of new phenotypes by amino-acid substitutions; The clinical problem of ß-lactam resistance in multi-drug resistant (MDR) Klebsiella pneumoniae, Acinetobacter baumanii & Pseudomonas aeruginosa; Interplay between ß-lactamase activity, membrane permeability & active efflux systems.