دورية أكاديمية
أعرض في EDS

Overcoming differences: The catalytic mechanism of metallo-β-lactamases.

التفاصيل البيبلوغرافية
العنوان: Overcoming differences: The catalytic mechanism of metallo-β-lactamases.
المؤلفون: Meini MR; Área Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 570, 200 Rosario, Argentina., Llarrull LI; Área Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 570, 200 Rosario, Argentina; Instituto de Biología Molecular y Celular de Rosario (IBR, CONICET-UNR), Predio CONICET Rosario, 2000 Rosario, Argentina. Electronic address: llarrull@ibr-conicet.gov.ar., Vila AJ; Área Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 570, 200 Rosario, Argentina; Instituto de Biología Molecular y Celular de Rosario (IBR, CONICET-UNR), Predio CONICET Rosario, 2000 Rosario, Argentina. Electronic address: vila@ibr-conicet.gov.ar.
المصدر: FEBS letters [FEBS Lett] 2015 Nov 14; Vol. 589 (22), pp. 3419-32. Date of Electronic Publication: 2015 Aug 20.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review
اللغة: English
بيانات الدورية: Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-3468 (Electronic) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE
أسماء مطبوعة: Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.
Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies.
مواضيع طبية MeSH: Biocatalysis*, beta-Lactamases/*metabolism, Bacteria/drug effects ; Bacteria/enzymology ; Crystallography, X-Ray ; Drug Resistance, Microbial ; Humans ; Hydrolysis ; beta-Lactamases/chemistry
مستخلص: Metallo-β-lactamases are the latest resistance mechanism of pathogenic and opportunistic bacteria against carbapenems, considered as last resort drugs. The worldwide spread of genes coding for these enzymes, together with the lack of a clinically useful inhibitor, have raised a sign of alarm. Inhibitor design has been mostly impeded by the structural diversity of these enzymes. Here we provide a critical review of mechanistic studies of the three known subclasses of metallo-β-lactamases, analyzed at the light of structural and mutagenesis investigations. We propose that these enzymes present a modular structure in their active sites that can be dissected into two halves: one providing the attacking nucleophile, and the second one stabilizing a negatively charged reaction intermediate. These are common mechanistic elements in all metallo-β-lactamases. Nucleophile activation does not necessarily requires a Zn(II) ion, but a Zn(II) center is essential for stabilization of the anionic intermediate. Design of a common inhibitor could be therefore approached based in these convergent mechanistic features despite the structural differences.
(Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
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معلومات مُعتمدة: R01 AI100560 United States AI NIAID NIH HHS; 1R01AI100560 United States AI NIAID NIH HHS
فهرسة مساهمة: Keywords: Antibiotic resistance; Drug design; Mechanism; Metallo-β-lactamase; Zinc enzyme
المشرفين على المادة: EC 3.5.2.6 (beta-Lactamases)
تواريخ الأحداث: Date Created: 20150823 Date Completed: 20160215 Latest Revision: 20181113
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC4640939
DOI: 10.1016/j.febslet.2015.08.015
PMID: 26297824
قاعدة البيانات: MEDLINE
الوصف
تدمد:1873-3468
DOI:10.1016/j.febslet.2015.08.015