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Information on EC 2.3.1.191 - UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase
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EC Tree
2.3.1.191 UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferaseIUBMB Comments
The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia coli prefers (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] , but it does not have an absolute specificity for 14-carbon hydroxy fatty acids, as it can transfer other fatty acids, including odd-chain fatty acids, if they are available to the organism .
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Word Map
- 2.3.1.191
- acyltransferases
- lps
- francisella
- trachomatis
-
chlamydia
- lipopolysaccharide
- udp-n-acetylglucosamine
-
homotrimer
- drug development
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
+
a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
=
a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
+
Synonyms
eclpxd, lpxd1, lpxd2, ctlpxd, pa3646, udp-3-o-acyl-glucosamine n-acyltransferase, udp-3-o-(r-3-hydroxyacyl)-glucosamine acyltransferase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase
-
acyltransferase LpxD
EcLpxD
La0512
LpxD
LpxD1
Lpxd2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine N-acyltransferase
The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia coli prefers (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] [3], but it does not have an absolute specificity for 14-carbon hydroxy fatty acids, as it can transfer other fatty acids, including odd-chain fatty acids, if they are available to the organism [5].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxyarachidonoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2-N-((3R)-3-hydroxyarachidonoyl)-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
the external layer of the Gram-negative bacterial outer membrane is primarily composed of a protective, selectively permeable lipopolysaccharide. The biosynthesis of lipopolysaccharide relies on UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD), which transfers 3-hydroxy-arachidonic acid from acyl carrier protein to the 2' amine of UDP-3-O-myristoyl glucosamine. CtLpxD is expected to utilize R-3-hydroxyarachidonoyl-[acyl-carrier protein] and UDP-3-O-(myristoyl)-R-D-glucosamine, based on the predominant molecular species of Chlamydia trachomatis lipid A. This proposal is not validated by in vitro assays
-
-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis(3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
(R,S)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
wild-type LpxD prefers (R,S)-3-hydroxymyristoyl-[acyl-carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] by a factor of 3, whereas the M290A mutant has the opposite selectivity
-
-
?
(R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
wild-type LpxD prefers (R,S)-3-hydroxymyristoyl-[acyl-carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] by a factor of 3, whereas the M290A mutant has the opposite selectivity
-
-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
-
since only (R)-3-hydroxymyristate is found at the 2,3,2, and 3 positions of Escherichia coli lipid A, it is reassuring that both Escherichia coli acyltransferases display extraordinary specificity for (R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
-
myristoyl-[acyl-carrier protein] does not serve as an acyl donor for the overproduced UDP-3-O-((R)-3-hydroxymyristoyl)-GlcN N-acyltransferase
-
-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
a comparison of the lipid A structures shows that in Escherichia coli and Neisseria meningitidis, LpxD can be expected to have the same specificity, both adding 3-hydroxymyristoyl chains
-
-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis(3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
-
third step of lipid A biosynthesis
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-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis(3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
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compulsory ordered mechanism in which (3R)-3-hydroxymyristoyl-[acyl-carrier protein] binds prior to UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine. The product, UDP-2,3-diacylglucosamine, dissociates prior to acyl-carrier protein
-
-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
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-
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ir
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
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-
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ir
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
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-
-
-
ir
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
-
-
-
-
ir
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
-
the LpxD1 enzyme adds a 3-OH C18 acyl group at 37 °C (host), whereas the LpxD2 enzyme adds a 3-OH C16 acyl group at 18 °C (environment)
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-
ir
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
-
-
-
-
ir
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
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the LpxD1 enzyme adds a 3-OH C18 acyl group at 37 °C (host), whereas the LpxD2 enzyme adds a 3-OH C16 acyl group at 18 °C (environment)
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-
ir
additional information
?
-
His247 and His284 contribute to a mechanism involving nucleophilic attack by the amine of one substrate on the carbonyl carbon of an acyl carrier protein thioester conjugate
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-
?
additional information
?
-
-
His247 and His284 contribute to a mechanism involving nucleophilic attack by the amine of one substrate on the carbonyl carbon of an acyl carrier protein thioester conjugate
-
-
?
additional information
?
-
-
both LpxA and LpxD, from Escherichia coli are also able to incorporate odd-chain fatty acids into lipid A when grown in the presence of 1% propionic acid. When grown on 1% propionic acid lipid A also contains the odd-chain fatty acids tridecanoic acid (C13), pentadecanoic acid (C15), hydroxy tridecanoic acid (C13OH), and hydroxy pentadecanoic acid (C15OH). Escherichia coli lipid A acyltransferases do not have an absolute specificity for 14-carbon hydroxy fatty acids but can transfer fatty acids differing by one carbon unit if the fatty acid substrates are available
-
-
?
additional information
?
-
-
R-3-hydroxylauroyl-methylphosphopantetheine is a very poor substrate. The specific activity, measured at either 0.01 mM or 1 mM (3R)-3-hydroxylauroylmethylphosphopantetheine as the acyl donor, is more than 100fold lower than with 0.01 mM (3R)-3-hydroxymyristoyl-[acyl-carrier protein]
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-
?
additional information
?
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fluorescent enzyme assay, method optimization, overview
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-
?
additional information
?
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ordered-sequential reaction mechanism. Acyl-ACP binds first to free LpxD forming a binary complex. ACP associates with the ACP-recognition domain and the acyl-4'-phosphopantetheine group packs into the hydrophobic N-channel. UDP-acyl-GlcN binds next, which initiates acyl transfer. In the ternary product complex, the 4'-phosphopantetheine arm of hydrolysed-acyl-ACP completely encloses the reaction chamber, blocking UDP-diacyl-GlcN from leaving. By moving the 4'-phosphopantetheine group towards Met 290, the catalytic chamber opens up. This motion drives the eventual release of UDP-diacyl-GlcN and triggers conformational changes downstream of helix-II leading to holo-ACP dissociation
-
-
?
additional information
?
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lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity. Both LpxA and LpxD, from either Escherichia coli or Porphyromonas gingivalis are also able to incorporate odd-chain fatty acids into lipid A when grown in the presence of 1% propionic acid. The relaxed specificity of the Porphyromonas gingivalis lipid A acyltransferases and the substrate availability account for the lipid A structural clusters that differ by 14 mass units observed in Porphyromonas gingivalis lipopolysaccharide preparations
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxyarachidonoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2-N-((3R)-3-hydroxyarachidonoyl)-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
the external layer of the Gram-negative bacterial outer membrane is primarily composed of a protective, selectively permeable lipopolysaccharide. The biosynthesis of lipopolysaccharide relies on UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD), which transfers 3-hydroxy-arachidonic acid from acyl carrier protein to the 2' amine of UDP-3-O-myristoyl glucosamine. CtLpxD is expected to utilize R-3-hydroxyarachidonoyl-[acyl-carrier protein] and UDP-3-O-(myristoyl)-R-D-glucosamine, based on the predominant molecular species of Chlamydia trachomatis lipid A. This proposal is not validated by in vitro assays
-
-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis(3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
-
third step of lipid A biosynthesis
-
-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
-
since only (R)-3-hydroxymyristate is found at the 2,3,2, and 3 positions of Escherichia coli lipid A, it is reassuring that both Escherichia coli acyltransferases display extraordinary specificity for (R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
a comparison of the lipid A structures shows that in Escherichia coli and Neisseria meningitidis, LpxD can be expected to have the same specificity, both adding 3-hydroxymyristoyl chains
-
-
?
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
-
-
-
ir
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
-
-
-
ir
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
-
-
-
-
ir
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
-
-
-
-
ir
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]
-
-
-
-
ir
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3R)-3-hydroxylauroyl-methylphosphopantetheine
-
competitive inhibitor with respect to UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine and an uncompetitive inhibitor with respect to (3R)-3-hydroxymyristoyl-[acyl-carrier protein]
(3R)-3-hydroxylauroylmethylphosphopantetheine
-
uncompetitive inhibitor against (3R)-3-hydroxymyristoyl-[acyl-carrier protein] and a competitive inhibitor against UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
4-(2-chlorophenyl)-3-hydroxy-7,7-dimethyl-2-phenyl-7,8-dihydro-2H-pyrazolo[3,4-b]quinolin-5(6H)-one
-
acyl-carrier protein
-
competitive inhibitor with respect to (3R)-3-hydroxymyristoyl-[acyl-carrier protein] and a noncompetitive inhibitor with respect to UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
Ca2+
-
inhibition is overcome by the addition of excess (3R)-3-hydroxymyristoyl-[acyl-carrier protein]
RJPXD33
-
i.e. TNLYMLPKWDIP, peptide inhibitor, binds to both UDP-N-acetylglucosamine acyltransferase (LpxA, EC 2.3.1.129) and UDP-3-O-(acyl)-glucosamine acyltransferase. Comparison with binding to LpxA suggests overlap with the acyl-phosphopantetheine arm of acyl-ACP, thereby inhibiting acyl-ACP from binding to LpxD. RJPXD33 binds to LpxD without the prior binding of other ligands
UDP-2-N-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
noncompetitive inhibitor against both substrates
additional information
-
divalent cations inhibit (3R)-3-hydroxymyristoyl-[acyl-carrier protein]-dependent acylation but not (3R)-3-hydroxylauroylmethylphosphopantetheine-dependent acylation, indicating that the acidic recognition helix of (3R)-3-hydroxymyristoyl-[acyl-carrier protein] contributes to binding; Na+ and K+ ions do not inhibit LpxD activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
LpxD does not require the presence of a detergent for catalytic activity because the critical micelle concentrations of its substrates are likely to be above 0.1 mM
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Leptospira interrogans lpxD Homologue Is Required for Thermal Acclimatization and Virulence.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004 - 0.012
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
-
pH 8.0, 25°C, recombinant His6-tagged LpxD
additional information
additional information
-
steady-state kinetic analysis
-
0.0017
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme H276A
0.0032
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, wild-type enzyme
0.0034
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme H239A
0.0035
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme F41A
0.0038
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme K194A
0.005
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme Y47A
0.012
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme K46A
0.013
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme N233A
0.013
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme Q236A
0.047
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme D232A
0.074
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme R293A
0.00084
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme H239A
0.0036
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme R293A
0.0042
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme Q236A
0.0056
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme K194A
0.0063
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme H276A
0.0071
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme K46A
0.0078
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme Y47A
0.028
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme N233A
0.067
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme D232A
0.073
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme F41A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine
-
pH 8.0, 25°C, recombinant His6-tagged LpxD
additional information
additional information
-
steady-state kinetic analysis
-
0.032
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme H239A
0.73
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme H276A
1.4
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme N233A
1.9
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme D232A
4.1
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme F41A
5.7
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme K194A
8.9
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme R293A
12
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme Q236A
17
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme K46A
18
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme Y47A
23
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, wild-type enzyme
0.032
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme H239A
0.73
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme H276A
1.4
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme N233A
1.9
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme D232A
4.1
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme F41A
5.7
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme K194A
8.9
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme R293A
12
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme Q236A
17
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme K46A
18
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, mutant enzyme Y47A
23
UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.4
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme H239A
10.7
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme N233A
40.4
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme D232A
120.3
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme R293A
429
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme H276A
923
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme Q236A
1171
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme F41A
1417
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme K46A
1500
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme K194A
3600
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, mutant enzyme Y47A
7188
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]
-
pH 7.5, 30°C, wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
UDP-2-N-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, noncompetitive inhibition against (R)-3-hydroxymyristoyl-[acyl-carrier protein]
0.0094
UDP-2-N-(R-3-hydroxymyristoyl)-alpha-D-glucosamine
-
pH 7.5, 30°C, noncompetitive inhibition against UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
0.39
(3R)-3-hydroxylauroyl-methylphosphopantetheine
-
pH 7.5, 30°C, competitive inhibition with respect to UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
0.69
(3R)-3-hydroxylauroyl-methylphosphopantetheine
-
pH 7.5, 30°C, uncompetitive inhibition with respect to (3R)-3-hydroxymyristoyl-[acyl-carrier protein]
0.048
acyl-carrier protein
-
pH 7.5, 30°C, competitive inhibition with respect to (R)-3-hydroxymyristoyl-[acyl-carrier protein]
0.139
acyl-carrier protein
-
pH 7.5, 30°C, noncompetitive inhibitionr with respect to UDP-3-O-(R-3-hydroxymyristoyl)-alpha-D-glucosamine
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
about half of the LpxD protein is made of hexad repeats (26 repeating hexapeptides). The lpxD gene from Yersinia enterocolitica is sequenced and the deduced amino acid sequence is compared with the lpxD sequences of Escherichia coli and Salmonella typhimurium. The hexapeptide repeat pattern is a very conservative property of these enzymes. Even though the overall homology between the proteins is 58%, the homology in the first residue of each hexapeptide is 100%
SwissProt
brenda
Legionella pneumophila is unique among a number of bacteria in containing multiple paralogues of LpxD
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
growth temperatures of 18°C to 37°C
brenda
-
growth temperatures of 18°C to 37°C
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
LpxD proteins in Arabidopsis thaliana are targeted to the mitochondria, subcellular localization analysis, overview
brenda
-
LpxD proteins in Arabidopsis thaliana are targeted to the mitochondria, subcellular localization analysis, overview
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
enzyme activity of the temperature-sensitive firA mutant RL-25 is reduced to less than 10% of wild-type enzyme
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
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
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
the enzyme is involved in the lipid A biosynthesis in the plant
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 lipid A biosynthesis
metabolism
the enzyme is involved in lipid A biosynthesis in Gram-negative bacteria
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
-
the enzyme is involved in the lipid A biosynthesis in the plant
-
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
-
LpxD is essential for survival in Gram-negative bacteria
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
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
-
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
physiological function
overexpression of UDP-3-O-[3-hydroxylauroyl] glucosamine N-acyltransferase reduces the quorum sensing regulator LasR activity, swarming motility, protease production and virulence without any influence on growth. These effects by PA3646 overexpression are caused by decreased production of quorum sensing signal
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
-
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
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM