Iron center, substrate recognition and mechanism of peptide deformylase
about
Trapping conformational states along ligand-binding dynamics of peptide deformylase: the impact of induced fit on enzyme catalysisAntibiotic Activity and Characterization of BB-3497, a Novel Peptide Deformylase InhibitorCrystal structure of type II peptide deformylase from Staphylococcus aureusStructural variation and inhibitor binding in polypeptide deformylase from four different bacterial speciesCrystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesisThe crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleftStructure and Activity of Human Mitochondrial Peptide Deformylase, a Novel Cancer TargetUnderstanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpartThe role of formylated peptides and formyl peptide receptor 1 in governing neutrophil function during acute inflammationPeptide deformylase in Staphylococcus aureus: resistance to inhibition is mediated by mutations in the formyltransferase geneThermolysin and mitochondrial processing peptidase: how far structure-functional convergence goes.Peptide deformylase inhibitors as antibacterial agents: identification of VRC3375, a proline-3-alkylsuccinyl hydroxamate derivative, by using an integrated combinatorial and medicinal chemistry approach.The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacteriumSolvent-assisted slow conversion of a dithiazole derivative produces a competitive inhibitor of peptide deformylase.Ligand-induced changes in the structure and dynamics of Escherichia coli peptide deformylasePeptide deformylase as a target for new generation, broad spectrum antimicrobial agents.Resistance of Streptococcus pneumoniae to deformylase inhibitors is due to mutations in defB.N-alkyl urea hydroxamic acids as a new class of peptide deformylase inhibitors with antibacterial activityActive 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.The mismetallation of enzymes during oxidative stress.Peptide deformylase: a target for novel antibiotics?The crystal structure of mitochondrial (Type 1A) peptide deformylase provides clear guidelines for the design of inhibitors specific for the bacterial forms.How water molecules affect the catalytic activity of hydrolases--a XANES study of the local structures of peptide deformylase.Synthetic analogues of cysteinate-ligated non-heme iron and non-corrinoid cobalt enzymesConformational change in substrate binding, catalysis and product release: an open and shut case?Mononuclear iron enzymes are primary targets of hydrogen peroxide stressZinc is the metal cofactor of Borrelia burgdorferi peptide deformylase.Expression, crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Xanthomonas oryzae pv. oryzaeDelineation of alternative conformational states in Escherichia coli peptide deformylase via thermodynamic studies for the binding of actinonin.A unique peptide deformylase platform to rationally design and challenge novel active compounds.Peptide deformylase--a promising therapeutic target for tuberculosis and antibacterial drug discovery.Metalloproteomics, metalloproteomes, and the annotation of metalloproteins.Three consecutive arginines are important for the mycobacterial peptide deformylase enzyme activityThe C-terminal residue of phage Vp16 PDF, the smallest peptide deformylase, acts as an offset element locking the active conformation.Effect of 4-methoxy 1-methyl 2-oxopyridine 3-carbamide on Staphylococcus aureus by inhibiting UDP-MurNAc-pentapeptide, peptidyl deformylase and uridine monophosphate kinase.Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with altered ligand affinity.Steric and electronic control over the reactivity of a thiolate-ligated Fe(II) complex with dioxygen and superoxide: reversible mu-oxo dimer formation.Kinetics and thermodynamics of metal-binding to histone deacetylase 8.Geometric preferences in iron(II) and zinc(II) model complexes of peptide deformylase.External nickel inhibits epithelial sodium channel by binding to histidine residues within the extracellular domains of alpha and gamma subunits and reducing channel open probability.
P2860
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P2860
Iron center, substrate recognition and mechanism of peptide deformylase
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Iron center, substrate recognition and mechanism of peptide deformylase
@ast
Iron center, substrate recognition and mechanism of peptide deformylase
@en
Iron center, substrate recognition and mechanism of peptide deformylase
@nl
type
label
Iron center, substrate recognition and mechanism of peptide deformylase
@ast
Iron center, substrate recognition and mechanism of peptide deformylase
@en
Iron center, substrate recognition and mechanism of peptide deformylase
@nl
prefLabel
Iron center, substrate recognition and mechanism of peptide deformylase
@ast
Iron center, substrate recognition and mechanism of peptide deformylase
@en
Iron center, substrate recognition and mechanism of peptide deformylase
@nl
P2093
P2860
P3181
P356
P1476
Iron center, substrate recognition and mechanism of peptide deformylase
@en
P2093
P2860
P2888
P304
P3181
P356
10.1038/4162
P577
1998-12-01T00:00:00Z
P5875
P6179
1036850601