Enzymatic synthesis of lipid A molecules with four amide-linked acyl chains. LpxA acyltransferases selective for an analog of UDP-N-acetylglucosamine in which an amine replaces the 3"-hydroxyl group

Enzymatic synthesis of lipid A molecules with four amide-linked acyl chains. LpxA acyltransferases selective for an analog of UDP-N-acetylglucosamine in which an amine replaces the 3"-hydroxyl group

Item
http://www.wikidata.org/entity/Q37003328
A methylated phosphate group and four amide-linked acyl chains in leptospira interrogans lipid A. The membrane anchor of an unusual lipopolysaccharide that activates TLR2Lipid A modification systems in gram-negative bacteriaStructural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferaseStructural Basis for the Sugar Nucleotide and Acyl-Chain Selectivity of Leptospira interrogans LpxAQuantitative comparison of catalytic mechanisms and overall reactions in convergently evolved enzymes: implications for classification of enzyme functionAn alternative route for UDP-diacylglucosamine hydrolysis in bacterial lipid A biosynthesis.A Leptospira interrogans enzyme with similarity to yeast Ste14p that methylates the 1-phosphate group of lipid A.Expression cloning and periplasmic orientation of the Francisella novicida lipid A 4'-phosphatase LpxF.Endotoxin structures in the psychrophiles Psychromonas marina and Psychrobacter cryohalolentis contain distinctive acyl features.The origin of 8-amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N) in the lipopolysaccharide of Shewanella oneidensis.Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coliMechanistic analysis of ghrelin-O-acyltransferase using substrate analogs.Lipid A structural modifications in extreme conditions and identification of unique modifying enzymes to define the Toll-like receptor 4 structure-activity relationship.Altered linkage of hydroxyacyl chains in lipid A of Campylobacter jejuni reduces TLR4 activation and antimicrobial resistance.Oxidation and transamination of the 3"-position of UDP-N-acetylglucosamine by enzymes from Acidithiobacillus ferrooxidans. Role in the formation of lipid a molecules with four amide-linked acyl chains.Cj1123c (PglD), a multifaceted acetyltransferase from Campylobacter jejuni.Biosynthesis and structure-activity relationships of the lipid a family of glycolipids.
P2860

Enzymatic synthesis of lipid A molecules with four amide-linked acyl chains. LpxA acyltransferases selective for an analog of UDP-N-acetylglucosamine in which an amine replaces the 3"-hydroxyl group

Item
http://www.wikidata.org/entity/Q37003328
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 24 March 2004
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Enzymatic synthesis of lipid A ...... replaces the 3"-hydroxyl group
@en
Enzymatic synthesis of lipid A ...... eplaces the 3"-hydroxyl group.
@nl
type
label
Enzymatic synthesis of lipid A ...... replaces the 3"-hydroxyl group
@en
Enzymatic synthesis of lipid A ...... eplaces the 3"-hydroxyl group.
@nl
prefLabel
Enzymatic synthesis of lipid A ...... replaces the 3"-hydroxyl group
@en
Enzymatic synthesis of lipid A ...... eplaces the 3"-hydroxyl group.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P932
P356
P1433
P1476
Enzymatic synthesis of lipid A ...... replaces the 3"-hydroxyl group
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P932