ArticleAntimicrobial agents and chemotherapy2012
Systematic analysis of metallo-β-lactamases using an automated database.
Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 45 citations in OpenAlex.
- Antimicrobial Resistance: Enzymes, Proteins, and Computational Resources.Current pharmaceutical design · 2026Review
- Strategies to Name Metallo-β-Lactamases and Number Their Amino Acid Residues.Antibiotics (Basel, Switzerland) · 2023Review
- Carbapenemase-producing bacteria in food-producing animals, wildlife and environment: A challenge for human health.Italian journal of food safety · 2019Article
- Identification and reconstruction of novel antibiotic resistance genes from metagenomes.Microbiome · 2019Article
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- Shaping Substrate Selectivity in a Broad-Spectrum Metallo-β-Lactamase.Antimicrobial agents and chemotherapy · 2018Article
- Systematic Identification and Classification of β-Lactamases Based on Sequence Similarity Criteria: β-Lactamase Annotation.Evolutionary bioinformatics online · 2018Article
- Beta-lactamase database (BLDB) - structure and function.Journal of enzyme inhibition and medicinal chemistry · 2017Article
- Identification of 76 novel B1 metallo-β-lactamases through large-scale screening of genomic and metagenomic data.Microbiome · 2017Article
- Carbapenemase-Producing Enterobacteriaceae Recovered from the Environment of a Swine Farrow-to-Finish Operation in the United States.Antimicrobial agents and chemotherapy · 2017Article
- Network Analysis of Sequence-Function Relationships and Exploration of Sequence Space of TEM β-Lactamases.Antimicrobial agents and chemotherapy · 2016Article
- Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution.Antimicrobial agents and chemotherapy · 2015Article
- How structural and physicochemical determinants shape sequence constraints in a functional enzyme.PloS one · 2015Article
- Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution.Antibiotics (Basel, Switzerland) · 2014Article
- Draft Genome Sequence of Elizabethkingia meningoseptica Isolated from a Traumatic Wound.Genome announcements · 2014Article
- Protein variants form a system of networks: microdiversity of IMP metallo-beta-lactamases.PloS one · 2014Article
- New β-lactamase inhibitors: a therapeutic renaissance in an MDR world.Antimicrobial agents and chemotherapy · 2014Review
- Solution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R-thiomandelic acid.The Biochemical journal · 2013Article
- New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamases.Bioorganic & medicinal chemistry letters · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metallo-β-lactamases (MBLs) are enzymes that hydrolyze β-lactam antibiotics, resulting in bacterial resistance to these drugs. These proteins have caused concerns due to their facile transference, broad substrate spectra, and the absence of clinically useful inhibitors. To facilitate the classification, nomenclature, and analysis of MBLs, an automated database system was developed, the Metallo-β-Lactamase Engineering Database (MBLED) (http://www.mbled.uni-stuttgart.de). It contains information on MBLs retrieved from the NCBI peptide database while strictly following the nomenclature by Jacoby and Bush (http://www.lahey.org/Studies/) and the generally accepted class B β-lactamase (BBL) standard numbering scheme for MBLs. The database comprises 597 MBL protein sequences and enables systematic analyses of these sequences. A systematic analysis employing the database resulted in the generation of mutation profiles of assigned IMP- and VIM-type MBLs, the identification of five MBL protein entries from the NCBI peptide database that were inconsistent with the Jacoby and Bush nomenclature, and the identification of 15 new IMP candidates and 9 new VIM candidates. Furthermore, the database was used to identify residues with high mutation frequencies and variability (mutation hot spots) that were unexpectedly distant from the active site located in the ββ sandwich: positions 208 and 266 in the IMP family and positions 215 and 258 in the VIM family. We expect that the MBLED will be a valuable tool for systematically cataloguing and analyzing the increasing number of MBLs being reported.
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