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Information on EC 2.3.1.241 - Kdo2-lipid IVA acyltransferase
for references in articles please use BRENDA:EC2.3.1.241
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.241 Kdo2-lipid IVA acyltransferase
IUBMB Comments
The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached to the nitrogen of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for lauryl (C12) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates.
The enzyme appears in viruses and cellular organisms
- 2.3.1.241
- neisseria
- meningitidis
- meningococcal
- lipopolysaccharide
-
bactericidal
-
penta-acylated
-
nomvs
-
hexa-acylated
-
endotoxic
-
serogrouping
- poras
- lipooligosaccharide
-
reactogenicity
-
monophosphoryl
-
underacylated
-
detergent-treated
-
2'-position
-
tetra-acylated
- drug development
Reaction Schemes
show+
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+
+
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+
Synonyms
lpxl1, lpxl2, pa0011, htrb1, pp_1735, esa02293, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(Kdo)2-lipid IVA lauroyltransferase
-
-
-
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alpha-Kdo-(2->4)-alpha-(2->6)-lipid IVA lauroyltransferase
-
-
-
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dodecanoyl-[acyl-carrier protein]:alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA O-dodecanoyltransferase
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-
-
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dodecanoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-dodecanoyltransferase
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-
-
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ESA02293
htrB
Kdo2-lipid IVA lauroyltransferase
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-
-
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lauroyl-[acyl-carrier protein]:Kdo2-lipid IVA O-lauroyltransferase
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-
-
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lipid A biosynthesis lauroyltransferase
LpxL
lpxL_1
lpxL_2
htrB
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-
-
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LpxL
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a fatty acyl-[acyl-carrier protein] + an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[lipid IVA] = an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(acyl)-[lipid IVA] + an [acyl-carrier protein]
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
(Kdo)2-lipid A biosynthesis (E. coli), (Kdo)2-lipid A biosynthesis (generic), (Kdo)2-lipid A biosynthesis (H. pylori), (Kdo)2-lipid A biosynthesis (P. gingivalis), (Kdo)2-lipid A biosynthesis (P. putida), (Kdo)2-lipid A biosynthesis I (Brucella), Kdo-lipid A biosynthesis (Vibrio cholerae serogroup O1 El Tor), superpathway of (Kdo)2-lipid A biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
fatty acyl-[acyl-carrier protein]:alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[lipid IVA] O-acyltransferase
The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached to the nitrogen of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for lauryl (C12) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
a dodecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA
dodecanoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
a tetradecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA
tetradecanoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
Substrates: i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. Kdo i.e. 3-deoxy-D-manno-octulosonic acid. The enzyme transfers laurate from lauroyl-acyl carrier protein to the 2'-R-3-hydroxymyristate moiety of the tetraacylated lipid A precursor Kdo2-lipid IVA. The enzyme catalyzes also a slow second acylation, generating Kdo2-(dilauroyl)-lipid IVA. The enzyme is capable of acylating lipid IVA in vitro. The specific activity with lipid IVA as the substrate is 6000fold lower than for Kdo2-lipid IVA. The presence of the Kdo disaccharide in the substrate accelerates laurate transfer by at least 3 orders of magnitude. The enzyme acylates the lipid A analogue 1-dephospho-Kdo2-lipid IVA with 10fold higher specific activity as compared to alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. Lauroyl-CoA can serve as an alternative acyl donor. Decanoyl-CoA, and to a lesser extent myristoyl-CoA, also function as acyl donors at low concentrations with inhibition of acylation at higher concentrations. Palmitoyl-CoA is inefficiently utilized as an acyl donor, but some acylation is observed. R-3-hydroxymyristoyl-[acyl-carrier protein] and synthetic R-3-hydroxylauroylmethylphosphopantetheine are poor acyl chain donors
Products: -
Products: -
?
a dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
Substrates: -
Products: LpxL transfers a C14:0 secondary acyl chain to the 2'-position of lipid A
Products: LpxL transfers a C14:0 secondary acyl chain to the 2'-position of lipid A
?
a dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
Substrates: -
Products: LpxL transfers a C14:0 secondary acyl chain to the 2'-position of lipid A
Products: LpxL transfers a C14:0 secondary acyl chain to the 2'-position of lipid A
?
a dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
Substrates: -
Products: -
Products: -
?
a dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
-
Substrates: i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
Products: -
Products: -
?
a dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
-
Substrates: the purified enzyme rapidly incorporates one dodecanoate into alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. The rate of dodecanoate incorporation is reduced by several orders of magnitude when either one or both Kdos are absent in the acceptor. The enzyme incorporates dodecanoate 38 times faster than decanoate or tetradecanoate, respectively. Transfer of palmitate, palmitoleate, or R-3-hydroxymyristate is very slow
Products: -
Products: -
?
a dodecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA
dodecanoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
Substrates: LpxL1 transfers a C12:0 acyl chain to the 2-O at the (3R)-hydroxytetradecanoyl chain on the 2'-glucosaminyl moity of Kdo2-lipid IVA
Products: -
Products: -
?
a dodecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA
dodecanoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
Substrates: -
Products: -
Products: -
?
a dodecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA
dodecanoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
Substrates: LpxL1 transfers a C12:0 acyl chain to the 2-O at the (3R)-hydroxytetradecanoyl chain on the 2'-glucosaminyl moity of Kdo2-lipid IVA
Products: -
Products: -
?
a dodecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA
dodecanoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
Substrates: acyltransferase encoded by PP_1735 catalyses the addition of the C12:0 chain to the 2'-position of lipid A in Pseudomonas putida
Products: -
Products: -
?
a tetradecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA
tetradecanoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
Substrates: -
Products: -
Products: -
?
a tetradecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA
tetradecanoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
Substrates: -
Products: -
Products: -
?
a tetradecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA
tetradecanoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: isoform HtrB1 exclusively mediates the addition of the 2-hydroxylaurate in C-2 position of lipid IVaA, while HtrB2 adds the laurate in C-2' position
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform HtrB1 exclusively mediates the addition of the 2-hydroxylaurate in C-2 position of lipid IVaA, while HtrB2 adds the laurate in C-2' position
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
a dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
Substrates: -
Products: -
Products: -
?
a dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
-
Substrates: i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
MgCl2
-
in the presence of 1 or 5 mM MgCl2, the enzyme shows a dependence on added detergent. At 5 mM MgCl2, the Triton X-100 optimum is considerably broad and therefore 5 mM MgCl2 is included in the assays
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
decanoyl-CoA
functions as acyl donor at low concentration with inhibition of acylation at higher concentrations
tetradecanoyl-CoA
i.e. myristoyl-CoA, functions as acyl donor at low concentration with inhibition of acylation at higher concentrations
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
greatly enhances the activity of the enzyme at lower concentrations, but the activity declines only gradually as the concentration of detergent increases
Triton X-100
-
in the presence of 1 or 5 mM MgCl2, the enzyme shows a dependence on added detergen. With Triton X-100, the highest activity is observed between 0.1 and 0.2% (w/v). At higher Triton X-100 concentrations, the activity dropps off, presumably because of surface dilution of the substrate in mixed micelles. At 5 mM MgCl2, the Triton X-100 optimum is considerably broader
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Arthritis
Neisseria meningitidis lipid A mutant LPSs function as LPS antagonists in humans by inhibiting TLR 4-dependent cytokine production.
Exanthema
Naturally occurring lipid A mutants in neisseria meningitidis from patients with invasive meningococcal disease are associated with reduced coagulopathy.
Hepatitis B
Enhancement of T-helper type I immune responses against hepatitis B surface antigen by LPS derivatives adjuvanted liposomes delivery system.
Infections
The structure of Neisseria meningitidis lipid A determines outcome in experimental meningococcal disease.
Influenza, Human
Incorporation of LpxL1, a detoxified lipopolysaccharide adjuvant, in influenza H5N1 virosomes increases vaccine immunogenicity.
Meningitis, Meningococcal
Naturally occurring lipid A mutants in neisseria meningitidis from patients with invasive meningococcal disease are associated with reduced coagulopathy.
Meningococcal Infections
The Neisseria meningitidis lpxL1 mutant induces less tissue factor expression and activity in primary human monocytes and monocyte-derived microvesicles than the wild type meningococcus.
Meningococcal Infections
Whole-blood incubation with the Neisseria meningitidis lpxL1 mutant induces less pro-inflammatory cytokines than the wild type, and IL-10 reduces the MyD88-dependent cytokines.
Neoplasms
Characterization of native outer membrane vesicles from lpxL mutant strains of Neisseria meningitidis for use in parenteral vaccination.
Neoplasms
Modification of lipid A biosynthesis in Neisseria meningitidis lpxL mutants: influence on lipopolysaccharide structure, toxicity, and adjuvant activity.
Tetanus
Neisseria meningitidis native outer membrane vesicles containing different lipopolysaccharide glycoforms as adjuvants for meningococcal and nonmeningococcal antigens.
Whooping Cough
A novel secondary acyl chain in the lipopolysaccharide of Bordetella pertussis required for efficient infection of human macrophages.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH 7.5, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
131
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH 7.5, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
lipid A produced by the lpxL2 mutant lacks the 2-hydroxymyristate, palmitate, and 4-aminoarabinose decorations found in the lipid A synthesized by the wild type. The lack of 2-hydroxymyristate is expected since LpxO modifies the myristate transferred by LpxL2 to the lipid A. The absence of the other two decorations is most likely caused by the downregulation of phoPQ and pmrAB expression
physiological function
physiological function
-
at 37°C and 42°C, lpxL mutants appear to activate different acyltransferases or biosynthetic pathways that generate atypical penta- and hexaacyl lipid A structures by incorporating longer fatty acids, such as a secondary palmitoleic acid (2'-O-position, distal) and a secondary palmitic acid (2-O-position, proximal), respectively. E.scherichia coli (lpxL) lipid A biosynthesis, and specifically the late acylation of lipid A, is temperature dependent and highly regulated
physiological function
a HtrB1 deletion mutant shows a decrease in 2-hydroxylaurate content in lipid A and otherwise similar growth characteristics as compared to wuild-type at all growth temperatures. A Htr2 deletion mutant shows a decrease in laurate content in lipid A and a major growth defect at 25°C and minor defects at 37 and 42°C. The htrB2 mutant shows increased susceptibility to both polymyxin B and colistin. HtrB1 and Htrb2 mutants display increased membrane permeability
physiological function
the enzyme might play an important role in the biosynthesis of lipid A and the innate immune system recognition in Klebsiella pneumoniae
physiological function
LpxL2-dependent lipid A acylation protects Klebsiella from polymyxins, mediates resistance to phagocytosis, limits the activation of inflammatory responses by macrophages, and is required for pathogen survival in the wax moth (Galleria mellonella). LpxL2 contribution to virulence is dependent on LpxO-mediated hydroxylation of the LpxL2-transferred myristate
physiological function
-
the enzyme might play an important role in the biosynthesis of lipid A and the innate immune system recognition in Klebsiella pneumoniae
-
Show AA Sequence and Transmembrane Helices (3748 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
LpxL monomer embeded in micelle of 12 n-dodecyl-beta-D-maltopyranoside molecules, gel filtration, mass spectrometry
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the addition of 50 mM NaCl together with 5 mM MgCl2 to the reaction mixture stabilizes the enzyme to preincubation
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme (LpxL1) is negatively regulated by the two-component system PhoPQ
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
LpxL2 might be a candidate target in the development of anti-Klebsiella pneumoniae drugs
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Six, D.A.; Carty, S.M.; Guan, Z.; Raetz, C.R.
Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis
Biochemistry
47
8623-8637
2008
Escherichia coli (P0ACV0)
brenda
Clementz, T.; Bednarski, J.J.; Raetz, C.R.
Function of the htrB high temperature requirement gene of Escherchia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate
J. Biol. Chem.
271
12095-12102
1996
Escherichia coli
brenda
Cai, L.; Li, Y.; Tao, G.; Guo, W.; Zhang, C.; Wang, X.
Identification of three genes encoding for the late acyltransferases of lipid A in Cronobacter sakazakii
Mar. Drugs
11
377-386
2013
Cronobacter sakazakii (A7ME71), Cronobacter sakazakii, Cronobacter sakazakii ATCC BAA-894 (A7ME71)
brenda
Schilling, B.; Hunt, J.; Gibson, B.W.; Apicella, M.A.
Site-specific acylation changes in the lipid A of Escherichia coli lpxL mutants grown at high temperatures
Innate Immun.
20
269-282
2014
Escherichia coli
brenda
Hittle, L.E.; Powell, D.A.; Jones, J.W.; Tofigh, M.; Goodlett, D.R.; Moskowitz, S.M.; Ernst, R.K.
Site-specific activity of the acyltransferases HtrB1 and HtrB2 in Pseudomonas aeruginosa lipid A biosynthesis
Pathog. Dis.
73
ftv053
2015
Pseudomonas aeruginosa (Q9I7B5), Pseudomonas aeruginosa
brenda
Li, Y.; Yun, J.; Liu, L.; Li, Y.; Wang, X.
Identification of two genes encoding for the late acyltransferases of lipid A in Klebsiella pneumoniae
Curr. Microbiol.
73
732-738
2016
Klebsiella pneumoniae (B5XXK1), Klebsiella pneumoniae (B5Y0A8), Klebsiella pneumoniae, Klebsiella pneumoniae 342 (B5XXK1), Klebsiella pneumoniae 342 (B5Y0A8)
brenda
Mills, G.; Dumigan, A.; Kidd, T.; Hobley, L.; Bengoechea, J.
Identification and characterization of two Klebsiella pneumoniae lpxL lipid A late acyltransferases and their role in virulence
Infect. Immun.
85
e00068-17
2017
Klebsiella pneumoniae (W9BFU2), Klebsiella pneumoniae (W9B4X1), Klebsiella pneumoniae
brenda
Zhu, L.; Li, Y.; Wang, J.; Wang, X.
Identification of two secondary acyltransferases of lipid A in Pseudomonas putida KT2442
J. Appl. Microbiol.
123
478-490
2017
Pseudomonas putida (Q88M40), Pseudomonas putida
brenda
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