2.3.1.191	malfunction	enzyme activity of the temperature-sensitive firA mutant RL-25 is reduced to less than 10% of wild-type enzyme	698693	
2.3.1.191	malfunction	lpxD mutant is susceptible to vancomycin and teicoplanin	695627	
2.3.1.191	malfunction	lpxD1-null mutant with shorter acyl chains in lipid A is more sensitive to various environmental stresses than Francisella novicida and lpxD2-null mutant	757609	
2.3.1.191	malfunction	the lpxD1-null mutant is attenuated in C57BL/6 mice and subsequently exhibits protection against a lethal wild-type challenge. The lpxD1-null and lpxD2-null mutant strains show altered antibiotic susceptibility patterns, membrane permeability, but no innate immune responses. The DELTAlpxD1 mutant is more susceptible to antibiotics with diverse mechanisms of action such as chloramphenicol, carbenicillin, ciprofloxacin, erythromycin, rifampin, and vancomycin, whereas the DELTAlpxD2 mutant is only susceptible to carbenicillin and erythromycin	-, 720944	
2.3.1.191	metabolism	Francisella modifies its lipid A structure in response to temperature adaptation by altering the length of the amidelinked acyl chains: 3-OH-C16 at environmental temperature and 3-OH-C18 at mammalian temperature	-, 720944	
2.3.1.191	metabolism	LpxD catalyzes the third step of lipid A biosynthesis, an acyl-acyl carrier protein (ACP)-dependent transfer of a fatty acyl moiety to a UDP-glucosamine core ring, overview	718571	
2.3.1.191	metabolism	quantitative model of the nine enzyme-catalyzed steps of Escherichia coli lipid A biosynthesis. Biosynthesis regulation occurs through regulated degradation of the LpxC and WaaA enzymes. LpxC, EC 3.5.1.108, is the rate-limiting enzyme if pathway regulation is ignored, but LpxK, EC 2.7.1.130, is the rate-limiting enzyme if pathway regulation is present, as it is in real cells	737072	
2.3.1.191	metabolism	the enzyme is involved in lipid A biosynthesis	757609	
2.3.1.191	metabolism	the enzyme is involved in lipid A biosynthesis in Gram-negative bacteria	755699	
2.3.1.191	metabolism	the enzyme is involved in the lipid A biosynthesis in the plant	-, 720913	
2.3.1.191	physiological function	a loss-of-expression mutant of lpxD is defective for biofilm formation on biotic and abiotic surfaces. The mutant strain exhibits significantly decreased bacterial attachment to cultured airway epithelial cells, as well as increased bacterial cytotoxicity toward airway cells. Airway cells incubated with the lpxD mutant or with mutant lipid A extracts exhibit decreased IL-8 production and necrosis, respectively	-, 735568	
2.3.1.191	physiological function	functional LpxD is essential for bacterial viability, transcriptional control of the lpxD genes, encoding the lipid A-modifying N-acyltransferase enzymes LpxD1/2,and posttranslational control of the LpxD1 and LpxD2 enzymatic activities are involved in the mechanism for temperature-regulated membrane remodeling by LPS/lipid A-level modifications resulting in alterations of membrane fluidity, as well as integrity, that may represent a general paradigm for bacterial membrane adaptation and virulence-state adaptation	-, 720944	
2.3.1.191	physiological function	inactivation of isoform la0512/LpxD1, imparts sensitivity to the host physiological temperature (37°C) and renders the bacteria avirulent in an animal infection model. The LpxD1 mutant displays compromised outer membrane integrity at host physiological temperature, but only minor changes in the lipid A moiety compared to that found in the wild-type strain. An in trans complementation restores the phenotypes to a level comparable to that of the wild-type strain	-, 736235	
2.3.1.191	physiological function	LpxD is essential for survival in Gram-negative bacteria	718571	
2.3.1.191	physiological function	LpxD is part of the biosynthesis pathway of lipid A and is responsible for transferring 3-hydroxymyristic acid from the R-3-hydroxymyristoyl-acyl carrier protein to the 2-OH group of UDP-3-O-(3-hydroxymyristoyl) glucosamine. The first three enzymes responsible for Gram-negative bacterial cell-wall synthesis, LpxA, LpxC and LpxD, are all present as single copies and are essential for bacterial viability	718513	
2.3.1.191	physiological function	overexpression of UDP-3-O-[3-hydroxylauroyl] glucosamine N-acyltransferase reduces the quorum sensing regulator LasR activity, swarming motility, protease production and virulence without any influence on growth. These effects by PA3646 overexpression are caused by decreased production of quorum sensing signal	736185