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Results 1 - 10 of 13 > >>
EC Number
General Information
Commentary
Reference
malfunction
enzyme activity of the temperature-sensitive firA mutant RL-25 is reduced to less than 10% of wild-type enzyme
malfunction
lpxD mutant is susceptible to vancomycin and teicoplanin
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
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
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
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
metabolism
the enzyme is involved in the lipid A biosynthesis in the plant
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
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
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
Results 1 - 10 of 13 > >>