2.3.1.129 G189S Escherichia coli strain SM101 is deficient in LpxA activity due to a G189S inactivating mutation. Enzymatic activity is restored when the mutant strain is transformed with a wild-type bearing plasmid is inactive 706784 2.3.1.129 G52L/R58L residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 G52V/R58V residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 G52W/R58W residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 G57P/N51P residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 H122A lower specific activity than wild-type 486258 2.3.1.129 H122N lower specific activity than wild-type 486258 2.3.1.129 H125A H125 is an important residue at the active site its mutation eliminates activity. Mutant shows significant growth reduction after introduction into Escherichia coli strain SM101 bearing a defective LpxA gene (G189S), and under novobiocin supplementation 706784 2.3.1.129 H125A lower specific activity than wild-type 486258 2.3.1.129 H125N lower specific activity than wild-type 486258 2.3.1.129 H144A lower specific activity than wild-type 486258 2.3.1.129 H144N lower specific activity than wild-type 486258 2.3.1.129 H160A lower specific activity than wild-type 486258 2.3.1.129 H160F lower specific activity than wild-type 486258 2.3.1.129 H53I/D59I residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 H53V/D59V residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 I20R mutation in the hydrophobic residue in the beta-helical core located in rung 2: LpxA is active 706784 2.3.1.129 I2R mutation in the hydrophobic residue in the beta-helical core located in rung 1: LpxA is active 706784 2.3.1.129 I38R mutation in the hydrophobic residue in the beta-helical core located in rung 3: LpxA is partially active 706784 2.3.1.129 I56A mutation in the hydrophobic core of the beta-helical domain: LpxA activity is not significantly affected compared to wild-type 706784 2.3.1.129 I56D/I62D residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 I56E/I62E residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 I56G mutation in the hydrophobic core of the beta-helical domain: LpxA activity is decreased compared to wild-type 706784 2.3.1.129 I56G/I62G residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 I56H/I62H residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 I56K/I62K residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 I56N mutation in the hydrophobic core of the beta-helical domain: LpxA activity is decreased compared to wild-type 706784 2.3.1.129 I56N/I62N residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 I56P/I62P residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 I56Q mutation in the hydrophobic core of the beta-helical domain: LpxA activity is decreased compared to wild-type 706784 2.3.1.129 I56Q/I62Q residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 I56R mutation in the hydrophobic core of the beta-helical domain: LpxA activity is completely abolished compared to wild-type 706784 2.3.1.129 I56R mutation in the hydrophobic residue in the beta-helical core located in rung 4: LpxA is inactive 706784 2.3.1.129 I56R/I62R residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 I56S/I62S residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 I56W/I62W residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 I56Y/I62Y residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 I86R mutation in the hydrophobic residue in the beta-helical core located in rung 5: LpxA is inactive 706784 2.3.1.129 I86R residue is located in the fifth rung of the beta-helical domain in the hydrophobic core of a beta helix, mutant is improperly folded, destabilized and its enzymatic activity is decreased. Mutant shows significant growth reduction after introduction into Escherichia coli strain SM101 bearing a defective LpxA gene (G189S), and under novobiocin supplementation 706784 2.3.1.129 K55D/E61D residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 K55P/E61P residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 K76A lower specific activity than wild-type 486258 2.3.1.129 K76R lower specific activity than wild-type 486258 2.3.1.129 additional information a recombinant prion protein-LpxA protein is generated, in which a PrP fragment that is thought to be essential for the conformational conversion is incorporated into the beta-helical domain of LpxA. Partial Lpxa enzymatic activity is observed, suggesting that the beta-helical structure may be able to accommodate a portion of the prion protein sequence and, as a corollary, that a prion protein fragment may adopt left-handed parallel beta helix (LbetaH) architecture 706784 2.3.1.129 additional information Arabidopsis thaliana lpxA complements an Escherichia coli mutant lacking the chromosomal lpxA and promotes the synthesis of lipid A in vivo similar to the lipid A produced in the presence of Escherichia coli lpxA 718930 2.3.1.129 additional information construction and characterization of an isogenic Moraxella catarrhalis lpxA mutant in strain O35E, which is viable despite the complete loss of cell surface lipooligosaccharides, the mutant strain shows significantly decreased toxicity in the Limulus amebocyte lysate assay, reduced resistance to normal human serum, reduced adherence to human epithelial cells, and enhanced clearance in lungs and nasopharynx in a mouse aerosol challenge model, phenotype, overview, the mutant elicits high levels of antibodies with bactericidal activity and provides protection against a challenge with the wild-type strain, thus the null LOS mutant is attenuated and may be a potential vaccine candidate against Moraxella catarrhalis -, 673981 2.3.1.129 additional information heterologous expression of Acidithiobacillus ferrooxidans' genes lpxA, gnnA, and gnnB results in occurence of UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose utilizing activity in Escherichia coli cells with defective lpxA gene in vivo 659349 2.3.1.129 P10A/P28A/P34A/P183A proline mutation at the turn region of the beta-helical domain: mutant shows lower activity compared to wild-type 706784 2.3.1.129 P28A/P34A proline mutation at the turn region of the beta-helical domain: mutant shows greater activity than the P10A/P28A/P34A/P183A mutant 706784 2.3.1.129 T54D/N60D residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 T54E/N60E residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 T54G/N60G residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 T54H/N60H residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 T54K/N60K residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 T54M/N60M residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 T54P/N60P residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 T54Q/N60Q residue tolerance in the beta-helical domain: mutation is tolerated 706784 2.3.1.129 T54R/N60R residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 T54W/N60W residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 T54Y/N60Y residue tolerance in the beta-helical domain: mutation is not tolerated 706784 2.3.1.129 V111R mutation in the hydrophobic residue in the beta-helical core located in rung 6: LpxA is inactive 706784 2.3.1.129 V129R mutation in the hydrophobic residue in the beta-helical core located in rung 7: LpxA is inactive 706784 2.3.1.129 Y66F/Y77F/Y219F/Y223F/Y243H all but one tyrosine residues are mutated. Mutant shows growth similar to wild-type after introduction into Escherichia coli strain SM101 bearing a defective LpxA gene (G189S), and under novobiocin supplementation 706784