Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
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Structural Basis for the Sugar Nucleotide and Acyl-Chain Selectivity of Leptospira interrogans LpxACrystal Structure and Acyl Chain Selectivity of Escherichia coli LpxD, the N -Acyltransferase of Lipid A BiosynthesisCrystal structure of LpxK, the 4'-kinase of lipid A biosynthesis and atypical P-loop kinase functioning at the membrane interfaceMechanistic Characterization of the Tetraacyldisaccharide-1-phosphate 4′-Kinase LpxK Involved in Lipid A BiosynthesisActivity and Crystal Structure of Arabidopsis thaliana UDP- N -Acetylglucosamine AcyltransferaseChasing acyl carrier protein through a catalytic cycle of lipid A productionA Complete Pathway Model for Lipid A Biosynthesis in Escherichia coliAn alternative route for UDP-diacylglucosamine hydrolysis in bacterial lipid A biosynthesis.Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspectiveDual targeting antibacterial peptide inhibitor of early lipid A biosynthesis.LPS remodeling is an evolved survival strategy for bacteria.Discovery of new biosynthetic pathways: the lipid A story.Pathway for lipid A biosynthesis in Arabidopsis thaliana resembling that of Escherichia coli.Toxic Accumulation of LPS Pathway Intermediates Underlies the Requirement of LpxH for Growth of Acinetobacter baumannii ATCC 19606.Dephosphorylated NPr is involved in an envelope stress response of Escherichia coliAcyltransferases in bacteria.Purification and characterization of the lipid A disaccharide synthase (LpxB) from Escherichia coli, a peripheral membrane proteinThe chain-flipping mechanism of ACP (acyl carrier protein)-dependent enzymes appears universal.Characterization of an Acinetobacter baumannii lptD Deletion Strain: Permeability Defects and Response to Inhibition of Lipopolysaccharide and Fatty Acid Biosynthesis.Structure, inhibition, and regulation of essential lipid A enzymes.Crystal structure and activity of Francisella novicida UDP-N-acetylglucosamine acyltransferase.LpxK Is Essential for Growth of Acinetobacter baumannii ATCC 19606: Relationship to Toxic Accumulation of Lipid A Pathway Intermediates.Kinetics and phospholipid specificity of apolipoprotein N-acyltransferaseA continuous fluorescent enzyme assay for early steps of lipid A biosynthesis.Structure of aryl O-demethylase offers molecular insight into a catalytic tyrosine-dependent mechanism.The Mechanism of Acetyl Transfer Catalyzed by Mycobacterium tuberculosis GlmU.A pathway-directed positive growth restoration assay to facilitate the discovery of lipid A and fatty acid biosynthesis inhibitors in Acinetobacter baumannii.
P2860
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P2860
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
description
2008 nî lūn-bûn
@nan
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Steady-state kinetics and mech ...... erase of lipid A biosynthesis.
@ast
Steady-state kinetics and mech ...... erase of lipid A biosynthesis.
@en
Steady-state kinetics and mech ...... erase of lipid A biosynthesis.
@nl
type
label
Steady-state kinetics and mech ...... erase of lipid A biosynthesis.
@ast
Steady-state kinetics and mech ...... erase of lipid A biosynthesis.
@en
Steady-state kinetics and mech ...... erase of lipid A biosynthesis.
@nl
prefLabel
Steady-state kinetics and mech ...... erase of lipid A biosynthesis.
@ast
Steady-state kinetics and mech ...... erase of lipid A biosynthesis.
@en
Steady-state kinetics and mech ...... erase of lipid A biosynthesis.
@nl
P2860
P356
P1433
P1476
Steady-state kinetics and mech ...... erase of lipid A biosynthesis.
@en
P2093
Christian R H Raetz
Craig M Bartling
P2860
P304
P356
10.1021/BI800240R
P407
P577
2008-04-19T00:00:00Z