UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism.
about
Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response.Lipid A modification systems in gram-negative bacteriaBinding 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 bindingCrystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitorSpecies-Specific and Inhibitor-Dependent Conformations of LpxC: Implications for Antibiotic DesignStructure 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 coliResidue ionization in LpxC directly observed by 67Zn NMR spectroscopy.3D-QSAR, Molecular Docking and Molecular Dynamics Simulation of Pseudomonas aeruginosa LpxC InhibitorsActive 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.Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis.Examination of mechanism of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) reveals unexpected role for dynamic tyrosineGeneral Base-General Acid Catalysis in Human Histone Deacetylase 8.Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase.The nucleotide-binding site of Aquifex aeolicus LpxC.Structure, inhibition, and regulation of essential lipid A enzymes.Synthesis, Structure, and SAR of Tetrahydropyran-Based LpxC Inhibitors.Crystal structure of A. aeolicus LpxC with bound product suggests alternate deacetylation mechanism.Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with altered ligand affinity.Catalysis by N-acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase (PIG-L) from Entamoeba histolytica: new roles for conserved residues.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.Uridine-based inhibitors as new leads for antibiotics targeting Escherichia coli LpxC.
P2860
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P2860
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism.
description
2005 nî lūn-bûn
@nan
2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
UDP-3-O-((R)-3-hydroxymyristoy ...... -base catalyst pair mechanism.
@ast
UDP-3-O-((R)-3-hydroxymyristoy ...... -base catalyst pair mechanism.
@en
type
label
UDP-3-O-((R)-3-hydroxymyristoy ...... -base catalyst pair mechanism.
@ast
UDP-3-O-((R)-3-hydroxymyristoy ...... -base catalyst pair mechanism.
@en
prefLabel
UDP-3-O-((R)-3-hydroxymyristoy ...... -base catalyst pair mechanism.
@ast
UDP-3-O-((R)-3-hydroxymyristoy ...... -base catalyst pair mechanism.
@en
P2093
P2860
P356
P1476
UDP-3-O-((R)-3-hydroxymyristoy ...... d-base catalyst pair mechanism
@en
P2093
Carol A Fierke
David W Christianson
Douglas A Whittington
Heather A Gennadios
Kristin M Rusche
P2860
P304
16969-16978
P356
10.1074/JBC.M413560200
P407
P577
2005-02-10T00:00:00Z