Natural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme Stability

Natural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme Stability

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http://www.wikidata.org/entity/Q28547682
Removal of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine β-Lactamases by Relieving Steric StrainPopulation Genomic Analysis of 1,777 Extended-Spectrum Beta-Lactamase-Producing Klebsiella pneumoniae Isolates, Houston, Texas: Unexpected Abundance of Clonal Group 307.Genomic epidemiology of global Klebsiella pneumoniae carbapenemase (KPC)-producing Escherichia coli.Deep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-β-Lactamase is Fragile to Mutations.A novel GoldNano Carb test for rapid phenotypic detection of carbapenemases, particularly OXA type, in Enterobacteriaceae, Pseudomonas aeruginosa and Acinetobacter spp.Multiregional dissemination of KPC-producing Klebsiella pneumoniae ST258/ST512 genotypes in Poland, 2010-14.Emergence of Ceftazidime-Avibactam Resistance Due to Plasmid-Borne blaKPC-3 Mutations during Treatment of Carbapenem-Resistant Klebsiella pneumoniae InfectionsEngineering Specificity from Broad to Narrow: Design of a β-Lactamase Inhibitory Protein (BLIP) Variant That Exclusively Binds and Detects KPC β-Lactamase.Vaborbactam: Spectrum of Beta-Lactamase Inhibition and Impact of Resistance Mechanisms on Activity in Enterobacteriaceae.Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2).Klebsiella pneumoniae Carbapenemase Producers in South Korea between 2013 and 2015.Adaptive benefits from small mutation supplies in an antibiotic resistance enzyme.Antimicrobial resistance (AMR) nanomachines-mechanisms for fluoroquinolone and glycopeptide recognition, efflux and/or deactivation.Structural and Mechanistic Basis for Extended-Spectrum Drug-Resistance Mutations in Altering the Specificity of TEM, CTX-M, and KPC β-lactamases.Ceftazidime Is the Key Diversification and Selection Driver of VIM-Type Carbapenemases.Optimization of Conformational Dynamics in an Epistatic Evolutionary Trajectory.Differential active site requirements for NDM-1 β-lactamase hydrolysis of carbapenem versus penicillin and cephalosporin antibiotics
P2860

Natural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme Stability

Item
http://www.wikidata.org/entity/Q28547682
description
2015 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի հունիսին հրատարակված գիտական հոդված
@hy
article scientifique
@fr
artículu científicu espublizáu en 2015
@ast
scientific article (publication date: June 2015)
@en
vedecký článok (publikovaný 2015-06)
@sk
vědecký článek publikovaný v roce 2015
@cs
wetenschappelijk artikel (gepubliceerd in 2015-06)
@nl
wissenschaftlicher Artikel
@de
наукова стаття, опублікована в червні 2015
@uk
name
Natural Variants of the KPC-2 ...... t the Cost of Enzyme Stability
@ast
Natural Variants of the KPC-2 ...... t the Cost of Enzyme Stability
@en
Natural Variants of the KPC-2 ...... t the Cost of Enzyme Stability
@nl
type
label
Natural Variants of the KPC-2 ...... t the Cost of Enzyme Stability
@ast
Natural Variants of the KPC-2 ...... t the Cost of Enzyme Stability
@en
Natural Variants of the KPC-2 ...... t the Cost of Enzyme Stability
@nl
prefLabel
Natural Variants of the KPC-2 ...... t the Cost of Enzyme Stability
@ast
Natural Variants of the KPC-2 ...... t the Cost of Enzyme Stability
@en
Natural Variants of the KPC-2 ...... t the Cost of Enzyme Stability
@nl
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P1476
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P478
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P5875
P698
P932
P3181
P356
P1433
P1476
Natural Variants of the KPC-2 ...... t the Cost of Enzyme Stability
@en
P2093
P2860
P304
P31
P3181
P356
10.1371/JOURNAL.PPAT.1004949
P407
P433
P478
P577
P5875
P698
P932