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Beta-lactamase database (BLDB) – structure and function

Authors :
Agustin Zavala
Thierry Naas
Rémy A. Bonnin
Laurent Dortet
Pascal Retailleau
Bogdan I. Iorga
Maria Laura Dabos
Saoussen Oueslati
Structure, Dynamique, Fonction Et Expression Des Beta-Lactamases À Large Spectre
Université Paris-Sud - Paris 11 - Faculté de médecine (UP11 UFR Médecine)
Université Paris-Sud - Paris 11 (UP11)-Université Paris-Sud - Paris 11 (UP11)-Centre National de Référence de la Résistance aux Antibiotiques (CNR)
Centre Hospitalier Régional Universitaire de Besançon (CHRU Besançon)-Centre Hospitalier Régional Universitaire de Besançon (CHRU Besançon)
Institut de Chimie des Substances Naturelles (ICSN)
Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)
This work was supported by the Laboratory of Excellence in Research on Medication and Innovative Therapeutics (LERMIT) [grant number ANR-10-LABX-33], by the JPIAMR transnational project DesInMBL [grant number ANR-14-JAMR-0002] and by the Région Ile-de-France (DIM Malinf).
ANR-11-IDEX-0003,IPS,Idex Paris-Saclay(2011)
ANR-14-JAMR-0002,DesInMBL,Structure-guided design of pan inhibitors of metallo-ß-lactamases(2014)
Source :
Journal of Enzyme Inhibition and Medicinal Chemistry, Journal of Enzyme Inhibition and Medicinal Chemistry, Informa Healthcare, 2017, 32 (1), pp.917-919. ⟨10.1080/14756366.2017.1344235⟩, Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 917-919 (2017)
Publication Year :
2017
Publisher :
Informa UK Limited, 2017.

Abstract

International audience; Beta-Lactamase Database (BLDB) is a comprehensive, manually curated public resource providing up-to-date structural and functional information focused on this superfamily of enzymes with a great impact on antibiotic resistance. All the enzymes reported and characterised in the literature are presented according to the class (A, B, C and D), family and subfamily to which they belong. All three-dimensional structures of b-lactamases present in the Protein Data Bank are also shown. The characterisation of representative mutants and hydrolytic profiles (kinetics) completes the picture and altogether these four elements constitute the essential foundation for a better understanding of the structure-function relationship within this enzymes family. BLDB can be queried using different protein-and nucleotide-based BLAST searches, which represents a key feature of particular importance in the context of the surveillance of the evolution of the antibiotic resistance. BLDB is available online at http://bldb.eu without any registration and supports all modern browsers.

Details

ISSN :
14756374 and 14756366
Volume :
32
Database :
OpenAIRE
Journal :
Journal of Enzyme Inhibition and Medicinal Chemistry
Accession number :
edsair.doi.dedup.....2ec67398f810ce7d1e2f8056f9bfa18a