EC Number   |
General Information |
Reference |
|---|
    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 | 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 | 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 | 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 | 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 | 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 | 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 |
