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Antibacterial activities and characterization of novel inhibitors of LpxC.

Antibacterial activities and characterization of novel inhibitors of LpxC.

http://www.wikidata.org/entity/Q31058699

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Lipid A modification systems in gram-negative bacteria Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis A universally applicable method of operon map prediction on minimally annotated genomes using conserved genomic context.Binding of Uridine 5‘-Diphosphate in the “Basic Patch” of the Zinc Deacetylase LpxC and Implications for Substrate Binding † , ‡Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: Time-dependent inhibition and specificity in ligand binding Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor Structure of the Bacterial Deacetylase LpxC Bound to the Nucleotide Reaction Product Reveals Mechanisms of Oxyanion Stabilization and Proton Transfer Structural Basis of the Promiscuous Inhibitor Susceptibility of Escherichia coli LpxC Lipid trafficking controls endotoxin acylation in outer membranes of Escherichia coli.Lipooligosaccharide is required for the generation of infectious elementary bodies in Chlamydia trachomatis.Residue ionization in LpxC directly observed by 67Zn NMR spectroscopy.Synergistic effect of imp/ostA and msbA in hydrophobic drug resistance of Helicobacter pylori.Challenges of antibacterial discovery LpxC inhibitors as new antibacterial agents and tools for studying regulation of lipid A biosynthesis in Gram-negative pathogens.UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism.Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis.Structure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptide.Whole-genome sequence of Chryseobacterium oranimense, a colistin-resistant bacterium isolated from a cystic fibrosis patient in France.Kdo2 -lipid A: structural diversity and impact on immunopharmacology.Inflammation--a new therapeutic target in pneumonia.Toxic Accumulation of LPS Pathway Intermediates Underlies the Requirement of LpxH for Growth of Acinetobacter baumannii ATCC 19606.Optimality principles reveal a complex interplay of intermediate toxicity and kinetic efficiency in the regulation of prokaryotic metabolism.Mutants resistant to LpxC inhibitors by rebalancing cellular homeostasis.A new class of UDP-3-O-(R-3-hydroxymyristol)-N-acetylglucosamine deacetylase (LpxC) inhibitors for the treatment of Gram-negative infections: PCT application WO 2008027466.Understanding efflux in Gram-negative bacteria: opportunities for drug discovery.Metalloenzyme inhibitors for the treatment of Gram-negative bacterial infections: a patent review (2009-2012).MsbA-dependent translocation of lipids across the inner membrane of Escherichia coli.Characterization of an Acinetobacter baumannii lptD Deletion Strain: Permeability Defects and Response to Inhibition of Lipopolysaccharide and Fatty Acid Biosynthesis.LpxC inhibitors: a patent review (2010-2016).Antibacterial Drug Discovery Targeting the Lipopolysaccharide Biosynthetic Enzyme LpxC.Structure, inhibition, and regulation of essential lipid A enzymes.FtsH-mediated coordination of lipopolysaccharide biosynthesis in Escherichia coli correlates with the growth rate and the alarmone (p)ppGpp.In Vitro and In Vivo Efficacy of an LpxC Inhibitor, CHIR-090, Alone or Combined with Colistin against Pseudomonas aeruginosa Biofilm.An Amphipathic Undecapeptide with All d-Amino Acids Shows Promising Activity against Colistin-Resistant Strains of Acinetobacter baumannii and a Dual Mode of Action.Mechanisms decreasing in vitro susceptibility to the LpxC inhibitor CHIR-090 in the gram-negative pathogen Pseudomonas aeruginosa.Conditional lethal amber mutations in essential Escherichia coli genes LpxK Is Essential for Growth of Acinetobacter baumannii ATCC 19606: Relationship to Toxic Accumulation of Lipid A Pathway Intermediates.Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in enterobacteria but not in all gram-negative bacteria.Inhibition of lipid A biosynthesis as the primary mechanism of CHIR-090 antibiotic activity in Escherichia coli.A slow, tight-binding inhibitor of the zinc-dependent deacetylase LpxC of lipid A biosynthesis with antibiotic activity comparable to ciprofloxacin.

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Antibacterial activities and characterization of novel inhibitors of LpxC.

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2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2002 թվականի հունիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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name

Antibacterial activities and characterization of novel inhibitors of LpxC.

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Antibacterial activities and characterization of novel inhibitors of LpxC.

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type

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Antibacterial activities and characterization of novel inhibitors of LpxC.

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Antibacterial activities and characterization of novel inhibitors of LpxC.

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Antibacterial activities and characterization of novel inhibitors of LpxC.

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Antibacterial activities and characterization of novel inhibitors of LpxC.

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AAC.46.6.1793-1799.2002

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Antimicrobial Agents and Chemotherapy

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Antibacterial activities and characterization of novel inhibitors of LpxC

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Fanny Coignard

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Ian Johnson

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Jac Wijkmans

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John M Clements

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Michael G Hunter

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Shilpa Palan

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Stephen Chandler

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P2860

Antibiotic Activity and Characterization of BB-3497, a Novel Peptide Deformylase Inhibitor

Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis

Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes

Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway

A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase.

UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme.

A mutant of Escherichia coli defective in the first step of endotoxin biosynthesis.

An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis.

The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis.

First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene

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1793-1799

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10.1128/AAC.46.6.1793-1799.2002

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6

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Andrew S. Waller

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12019092

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