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Results 1 - 10 of 14 > >>
EC Number
Amino acid exchange
Commentary
Reference
D232A
mutation causes a 10fold reduction in kcat and a striking increase in the KM for both substrates
F41A
mutation increases the KM for UDP-3-O-((3R)-3-hydroxymyristoyl)-a-D-glucosamine 30fold and kcat 5fold
K194A
mutation has little effect on activity
K46A
mutation causes 3fold increase in KM((3R)-3-hydroxymyristoyl-[acyl-carrier protein]) and has no effect on kcat
M290A
wild-type EcLpxD prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 3, whereas the M290A mutant has the opposite selectivity. Both wild-type and M290A EcLpxD rescue the conditional lethality of Escherichia coli RL25, a temperature-sensitive strain harboring point mutations in lpxD. Complementation with wild-type EcLpxD restores normal lipid A containing only N-linked hydroxymyristate to RL25 at 42°C, as judged by mass spectrometry, whereas the M290A mutant generates multiple lipid A species containing one or two longer hydroxy fatty acids in place of the usual (3R)-3-hydroxymyristate at positions 2 and 20
M292A
wild-type EcLpxD prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 3, mutant enzyme M292A prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 2.5
more
construction of lpx insertional knockout mutations or RNAi knock-down mutants
more
construction of lpxD1-null and lpxD2-null mutant strains, that show altered antibiotic susceptibility patterns, membrane permeability, but no innate immune responses
N233A
mutation causes a 10fold reduction in kcat and a striking increase in the KM for both substrates
N240A
causes less than a 2fold reduction in specific activity, when assayed at substrate concentrations at 2fold above KM with the purified proteins
Results 1 - 10 of 14 > >>