2.3.1.191: UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase
This is an abbreviated version!
For detailed information about UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.191
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2.3.1.191
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acyltransferases
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lps
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francisella
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trachomatis
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chlamydia
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lipopolysaccharide
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udp-n-acetylglucosamine
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homotrimer
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drug development
- 2.3.1.191
- acyltransferases
- lps
- francisella
- trachomatis
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chlamydia
- lipopolysaccharide
- udp-n-acetylglucosamine
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homotrimer
- drug development
Reaction
Synonyms
acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase, acyltransferase LpxD, CtLpxD, EcLpxD, firA, La0512, LpxD, LpxD1, Lpxd2, PA3646, UDP-3-O-(R-3-hydroxyacyl)-glucosamine acyltransferase, UDP-3-O-acyl-glucosamine N-acyltransferase
ECTree
2.3.1.191 UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.191 - UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D232A
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mutation causes a 10fold reduction in kcat and a striking increase in the KM for both substrates
F41A
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mutation increases the KM for UDP-3-O-((3R)-3-hydroxymyristoyl)-a-D-glucosamine 30fold and kcat 5fold
K46A
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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
N233A
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mutation causes a 10fold reduction in kcat and a striking increase in the KM for both substrates
N240A
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causes less than a 2fold reduction in specific activity, when assayed at substrate concentrations at 2fold above KM with the purified proteins
N44A
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causes less than a 2fold reduction in specific activity, when assayed at substrate concentrations at 2fold above KM with the purified proteins
Q32A
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causes less than a 2fold reduction in specific activity, when assayed at substrate concentrations at 2fold above KM with the purified proteins
R293A
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KM((3R)-3-hydroxymyristoyl-[acyl-carrier protein]) increases 23fold compared to wild-type with little effect on kcat
additional information
additional information
construction of lpx insertional knockout mutations or RNAi knock-down mutants
additional information
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construction of lpx insertional knockout mutations or RNAi knock-down mutants
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additional information
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construction of lpxD1-null and lpxD2-null mutant strains, that show altered antibiotic susceptibility patterns, membrane permeability, but no innate immune responses
additional information
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construction of lpxD1-null and lpxD2-null mutant strains, that show altered antibiotic susceptibility patterns, membrane permeability, but no innate immune responses
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