UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme.
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Lipid A modification systems in gram-negative bacteriaLipopolysaccharide endotoxinsCrystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesisLipid A as a Drug Target and Therapeutic MoleculeBinding of Uridine 5‘-Diphosphate in the “Basic Patch” of the Zinc Deacetylase LpxC and Implications for Substrate Binding † , ‡Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitorA Structure-Based Approach to Ligand Discovery for 2 C -Methyl- d -erythritol-2,4-cyclodiphosphate Synthase: A Target for Antimicrobial Therapy †Structures of Metal-Substituted Human Histone Deacetylase 8 Provide Mechanistic Inferences on Biological Function,Structure of the Metal-Dependent Deacetylase LpxC from Yersinia enterocolitica Complexed with the Potent Inhibitor CHIR-090,Structure of the Bacterial Deacetylase LpxC Bound to the Nucleotide Reaction Product Reveals Mechanisms of Oxyanion Stabilization and Proton TransferA Complete Pathway Model for Lipid A Biosynthesis in Escherichia coliAntibacterial activities and characterization of novel inhibitors of LpxC.Residue ionization in LpxC directly observed by 67Zn NMR spectroscopy.Challenges of antibacterial discoveryActive site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions.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.Discovery of new biosynthetic pathways: the lipid A story.Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.Biosynthesis, transport, and modification of lipid A.Glutathione Peroxidase of Pennisetum glaucum (PgGPx) Is a Functional Cd2+ Dependent Peroxiredoxin that Enhances Tolerance against Salinity and Drought StressToxic Accumulation of LPS Pathway Intermediates Underlies the Requirement of LpxH for Growth of Acinetobacter baumannii ATCC 19606.Helicobacter pylori Resists the Antimicrobial Activity of Calprotectin via Lipid A Modification and Associated Biofilm Formation.Mutants resistant to LpxC inhibitors by rebalancing cellular homeostasis.Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase.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.The lipopolysaccharide export pathway in Escherichia coli: structure, organization and regulated assembly of the Lpt machineryStructure, inhibition, and regulation of essential lipid A enzymes.High susceptibility of MDR and XDR Gram-negative pathogens to biphenyl-diacetylene-based difluoromethyl-allo-threonyl-hydroxamate LpxC inhibitors.Purification, substrate range, and metal center of AtzC: the N-isopropylammelide aminohydrolase involved in bacterial atrazine metabolism.Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with altered ligand affinity.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.A continuous fluorescent enzyme assay for early steps of lipid A biosynthesis.Molecular validation of LpxC as an antibacterial drug target in Pseudomonas aeruginosa.Antimicrobial activity of CHIR-090, an inhibitor of lipopolysaccharide biosynthesis, against the Burkholderia cepacia complex.Tyrosinase inhibitory effect of benzoic acid derivatives and their structure-activity relationships.Uridine-based inhibitors as new leads for antibiotics targeting Escherichia coli LpxC.Discrete divalent rare-earth cationic ROP catalysts: ligand-dependent redox behavior and discrepancies with alkaline-earth analogues in a ligand-assisted activated monomer mechanism.The LpxL acyltransferase is required for normal growth and penta-acylation of lipid A in Burkholderia cenocepacia.
P2860
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P2860
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme.
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
UDP-3-O-(R-3-hydroxymyristoyl) ...... coli is a zinc metalloenzyme.
@ast
UDP-3-O-(R-3-hydroxymyristoyl) ...... coli is a zinc metalloenzyme.
@en
type
label
UDP-3-O-(R-3-hydroxymyristoyl) ...... coli is a zinc metalloenzyme.
@ast
UDP-3-O-(R-3-hydroxymyristoyl) ...... coli is a zinc metalloenzyme.
@en
prefLabel
UDP-3-O-(R-3-hydroxymyristoyl) ...... coli is a zinc metalloenzyme.
@ast
UDP-3-O-(R-3-hydroxymyristoyl) ...... coli is a zinc metalloenzyme.
@en
P2093
P356
P1433
P1476
UDP-3-O-(R-3-hydroxymyristoyl) ...... coli is a zinc metalloenzyme.
@en
P2093
C A Fierke
J E Jackman
P304
P356
10.1021/BI982339S
P407
P577
1999-02-01T00:00:00Z