ReviewClinical microbiology reviews2016
A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes.
Review in Clinical microbiology reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
78 citing papers in PubMed.
- Characterization of GUA-1, a chromosomally encoded ESBL fromAntimicrobial agents and chemotherapy · 2026Article
- Vibrio Community Structure Shapes the Diversity of Carbenicillin-Hydrolysing Class A β-Lactamase Circulating in European Coastal Environments.Environmental microbiology · 2026Article
- Genomic Characterization, Antimicrobial Resistance Profiles, andAnimals : an open access journal from MDPI · 2026Article
- Integrated functional genomics and safety assessment of plant-growth-promoting Caryophanales from post-maize-cultivation soils.BMC genomics · 2026Article
- Synergistic Potential of Repurposing non-β-lactam Compounds as Class A serine β-lactamases Inhibitor: Insights from MolecularDocking, Molecular Dynamics Simulations and Antimicrobial Potentiation.Scientific reports · 2026Article
- A review on hypervirulent and multidrug-resistant Klebsiella pneumoniae: An emerging threat to human health.Naunyn-Schmiedeberg's archives of pharmacology · 2026Review
- Origins and breadth of pairwise epistasis in an α-helix of β-lactamase TEM-1.Nature communications · 2026Article
- Antibiotic: a boon to mankind and doom to the environment - an insight on biological and non-biological degradation processes.Frontiers in microbiology · 2026Review
- Structural comparison of substrate-binding pockets of serine β-lactamases in classes A, C, and D.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Strategic design of a multi-tier database for class A β-lactamase BlaC variants of M. tuberculosis: advancing the fight against antibacterial resistance.The Journal of antibiotics · 2025Article
- Genomic Analysis for the Safety Assessment of a Potential Probiotic Strain Pediococcus pentosaceus BBS1 Isolated From Lao Fermented Bamboo Shoots (Nor Mai Som).MicrobiologyOpen · 2025Article
- Genome-based classification of Paraniabella aurantiaca gen. nov., sp. nov., isolated from soil and taxonomic reclassification of five species within the genus Niabella.Journal of microbiology (Seoul, Korea) · 2025Article
- Catalytic Residue Reprogramming Enhances Enzyme Activity at Alkaline pH via Phenolate-Mediated Proton Transfer.ACS synthetic biology · 2025Article
- Unique Regulation of Sed-1 β-Lactamase inAntibiotics (Basel, Switzerland) · 2025Article
- OXA-204 Carbapenemase in Clinical Isolate of Pseudomonas guariconensis, Tunisia.Emerging infectious diseases · 2025Article
- Evolutionary Dynamics and Functional Differences in Clinically Relevant Pen β-Lactamases fromJournal of chemical information and modeling · 2025Article
- Investigation of antimicrobial susceptibility and resistance gene prevalence in Capnocytophaga spp. isolated from dogs and cats and characterization of novel class A β-lactamase CST-1.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Article
- The continued evolution of the L2 cephalosporinase in Stenotrophomonas maltophilia: a key driver of beta-lactam resistance.The Biochemical journal · 2025Article
- Revisiting the Metallo-International journal of microbiology · 2025Review
- Review
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For medical biologists, sequencing has become a commonplace technique to support diagnosis. Rapid changes in this field have led to the generation of large amounts of data, which are not always correctly listed in databases. This is particularly true for data concerning class A β-lactamases, a group of key antibiotic resistance enzymes produced by bacteria. Many genomes have been reported to contain putative β-lactamase genes, which can be compared with representative types. We analyzed several hundred amino acid sequences of class A β-lactamase enzymes for phylogenic relationships, the presence of specific residues, and cluster patterns. A clear distinction was first made between dd-peptidases and class A enzymes based on a small number of residues (S70, K73, P107, 130SDN132, G144, E166, 234K/R, 235T/S, and 236G [Ambler numbering]). Other residues clearly separated two main branches, which we named subclasses A1 and A2. Various clusters were identified on the major branch (subclass A1) on the basis of signature residues associated with catalytic properties (e.g., limited-spectrum β-lactamases, extended-spectrum β-lactamases, and carbapenemases). For subclass A2 enzymes (e.g., CfxA, CIA-1, CME-1, PER-1, and VEB-1), 43 conserved residues were characterized, and several significant insertions were detected. This diversity in the amino acid sequences of β-lactamases must be taken into account to ensure that new enzymes are accurately identified. However, with the exception of PER types, this diversity is poorly represented in existing X-ray crystallographic data.
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