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Information on EC 2.3.1.243 - acyl-Kdo2-lipid IVA acyltransferase
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EC Tree
2.3.1.243 acyl-Kdo2-lipid IVA acyltransferaseIUBMB 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 at the 2-O position of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for myristoyl (C14) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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Synonyms
esa01386, jhp0255, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ESA01386
lauroyl-Kdo2-lipid IVA myristoyltransferase
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lipid A biosynthesis myristoyltransferase
LpxL
LpxL2
LpxM
MsbB acyltransferase
myristoyl-[acyl-carrier protein]:alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(dodecanoyl)-lipid IVA O-myristoyltransferase
tetradecanoyl-[acyl-carrier protein]:dodecanoyl-Kdo2-lipid IVA O-tetradecanoyltransferase
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LpxM
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MsbB acyltransferase
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myristoyl-[acyl-carrier protein]:alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(dodecanoyl)-lipid IVA O-myristoyltransferase
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myristoyl-[acyl-carrier protein]:alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(dodecanoyl)-lipid IVA O-myristoyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a tetradecanoyl-[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-dodecanoyloxytetradecanoyl]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-(tetradecanoyloxy)tetradecanoyl]-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]
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SYSTEMATIC NAME
IUBMB Comments
fatty acyl-[acyl-carrier protein]:alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(acyl)-[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 at the 2-O position of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for myristoyl (C14) 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
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
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-dodecanoyloxytetradecanoyl]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-(dodecanoyloxy)tetradecanoyl]-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]
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a tetradecanoyl-[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-dodecanoyloxytetradecanoyl]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-(tetradecanoyloxy)tetradecanoyl]-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 tetradecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(tetradecanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
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dodecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(dodecanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
the enzyme possesses acyltransferase and acylprotein thioesterase activities. The enzyme displays a strong preference for dodecanoyl-[acyl-carrier protein] over the other acyl chain lengths tested
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?
hexadecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(hexadecanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
the enzyme possesses acyltransferase and acylprotein thioesterase activities. The enzyme displays a strong preference for dodecanoyl-[acyl-carrier protein] over the other acyl chain lengths tested
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?
octanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(octanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
the enzyme possesses acyltransferase and acylprotein thioesterase activities. The enzyme displays a strong preference for dodecanoyl-[acyl-carrier protein] over the other acyl chain lengths tested
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tetradecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(tetradecanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
the enzyme possesses acyltransferase and acylprotein thioesterase activities. The enzyme displays a strong preference for dodecanoyl-[acyl-carrier protein] over the other acyl chain lengths tested
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a tetradecanoyl-[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-dodecanoyloxytetradecanoyl]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-(tetradecanoyloxy)tetradecanoyl]-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]
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LpxM transfers a C14:0 secondary acyl chain to the 3'-position of lipid A
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?
a tetradecanoyl-[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-dodecanoyloxytetradecanoyl]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-(tetradecanoyloxy)tetradecanoyl]-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]
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LpxM transfers a C14:0 secondary acyl chain to the 3'-position of lipid A
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?
a tetradecanoyl-[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-dodecanoyloxytetradecanoyl]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-(tetradecanoyloxy)tetradecanoyl]-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]
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?
a tetradecanoyl-[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-dodecanoyloxytetradecanoyl]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-(tetradecanoyloxy)tetradecanoyl]-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]
decanoyl, palmitoyl, palmitoleoyl, and (R)-3-hydroxymyristoyl-[acyl-carrier protein] are poor acyl donors. The enzyme acylates (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-dodecanoyloxytetradecanoyl]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 about 100times faster than (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
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a tetradecanoyl-[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-dodecanoyloxytetradecanoyl]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-(tetradecanoyloxy)tetradecanoyl]-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]
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additional information
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the enzyme transfers a myristoyl chain to the (3R)-hydroxytetradecanoyl chain at the 3-O of the 2'-glucosaminyl moiety of Kdo2-lipid IV A
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additional information
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the enzyme transfers a myristoyl chain to the (3R)-hydroxytetradecanoyl chain at the 3-O of the 2'-glucosaminyl moiety of Kdo2-lipid IV A
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additional information
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enzyme LpxJ catalyzes the addition of a C12:0 or C14:0 acyl chain to the 3'-linked primary acyl chain of lipid IVA. LpxJ can act before the 2' secondary acyltransferase, LpxL, as well as the 3-deoxy-D-manno-octulosonic acid transferase, KdtA. LpxJ can only utilize acyl-ACPs rather than acyl coenzyme A, preferring C12:0-ACP and C14:0-ACP. No substrate: hexa-acylated substrate Kdo2-lipid A
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additional information
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enzyme LpxJ catalyzes the addition of a C12:0 or C14:0 acyl chain to the 3'-linked primary acyl chain of lipid IVA. LpxJ can act before the 2' secondary acyltransferase, LpxL, as well as the 3-deoxy-D-manno-octulosonic acid transferase, KdtA. LpxJ can only utilize acyl-ACPs rather than acyl coenzyme A, preferring C12:0-ACP and C14:0-ACP. No substrate: hexa-acylated substrate Kdo2-lipid A
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additional information
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lipid A in lipopolysaccharide of Escherichia coli mutant strains is modified by the introduction of myristoyltransferase gene cloned from Klebsiella pneumoniae. When the lpxL2 gene is introduced into the mutant having lipid A containing only 3-hydroxymyristic acids, it produces lipid A with two additional myristic acids (C14:0). When the same gene is introduced into the mutant with pentaacylated lipid A containing one lauric acid (C12:0), C12:0 is replaced by C14:0
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additional information
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Klebsiella pneumoniae NBRC 14940T
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lipid A in lipopolysaccharide of Escherichia coli mutant strains is modified by the introduction of myristoyltransferase gene cloned from Klebsiella pneumoniae. When the lpxL2 gene is introduced into the mutant having lipid A containing only 3-hydroxymyristic acids, it produces lipid A with two additional myristic acids (C14:0). When the same gene is introduced into the mutant with pentaacylated lipid A containing one lauric acid (C12:0), C12:0 is replaced by C14:0
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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
a tetradecanoyl-[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-dodecanoyloxytetradecanoyl]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-(tetradecanoyloxy)tetradecanoyl]-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]
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?
a tetradecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(tetradecanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001845
dodecanoyl-[acyl-carrier protein]
pH and temperature not specified in the publication
0.03047
hexadecanoyl-[acyl-carrier protein]
pH and temperature not specified in the publication
0.009887
octanoyl-[acyl-carrier protein]
pH and temperature not specified in the publication
0.01035
tetradecanoyl-[acyl-carrier protein]
pH and temperature not specified in the publication
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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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
the enzyme is necessary for the biosynthesis of lipid A, which comprises the outer leaflet of the outer membrane in Gram-negative bacteria. The enzyme has important effects on virulence in many human and animal pathogen
physiological function
malfunction
LpxL depletion caused reduced cell growth and defects in cell morphology
malfunction
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LpxL depletion caused reduced cell growth and defects in cell morphology
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physiological function
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a strain E058 lpxM mutant lacks one myristoyl (C14:0) on its lipid A molecules. No differences are observed between the mutant and wild-type in growth rate in different broths and ability to survive in specific-pathogen-free chicken serum. The mutant strain shows significantly reduced invasion and intracellular survival in the avian macrophage HD11 cell line. HD11 cells treated with E058 lpxM-mutant derived lipopolysaccharide also show reduction of nitric oxide production and downregulation of cytokine gene expression. Compared to the parental strain, the mutant leads to a significant reduction in bacterial load in heart, liver, spleen, lung, and kidney tissues. The histopathological lesions in visceral organs of birds challenged with the wild-type strain are more severe than in birds infected with the mutant. The mutant shows a sensitivity pattern similar to the parental strain following exposure to several hydrophobic reagents
physiological function
expression of LpxJ complements the defects of an Escherichia coli LpxM mutant
physiological function
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lipid A structures of lpxM and lpxP mutants lack the secondary lauroyl 12:0 group (R3'') or palmitoleoyl 16:1 group (R2''), respectively, and thus both represent a pentaacyl lipid A. Lipid A of Yersinia pestis lpxM/lpxP double mutant lacks both secondary acyl groups, 12:0 and 16:1, and is thus represented by the tetraacyl form. The absence of at least one acyl group is crucial for binding of lipopolysaccharide to toll-like receptor TLR4. Lipopolysaccharide from lpxM and and lpxP mutants induces TNF production at approximately the same level, the former being a slightly stronger activator than the latter
physiological function
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a strain E058 lpxM mutant lacks one myristoyl (C14:0) on its lipid A molecules. No differences are observed between the mutant and wild-type in growth rate in different broths and ability to survive in specific-pathogen-free chicken serum. The mutant strain shows significantly reduced invasion and intracellular survival in the avian macrophage HD11 cell line. HD11 cells treated with E058 lpxM-mutant derived lipopolysaccharide also show reduction of nitric oxide production and downregulation of cytokine gene expression. Compared to the parental strain, the mutant leads to a significant reduction in bacterial load in heart, liver, spleen, lung, and kidney tissues. The histopathological lesions in visceral organs of birds challenged with the wild-type strain are more severe than in birds infected with the mutant. The mutant shows a sensitivity pattern similar to the parental strain following exposure to several hydrophobic reagents
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physiological function
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lipid A structures of lpxM and lpxP mutants lack the secondary lauroyl 12:0 group (R3'') or palmitoleoyl 16:1 group (R2''), respectively, and thus both represent a pentaacyl lipid A. Lipid A of Yersinia pestis lpxM/lpxP double mutant lacks both secondary acyl groups, 12:0 and 16:1, and is thus represented by the tetraacyl form. The absence of at least one acyl group is crucial for binding of lipopolysaccharide to toll-like receptor TLR4. Lipopolysaccharide from lpxM and and lpxP mutants induces TNF production at approximately the same level, the former being a slightly stronger activator than the latter
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Show AA Sequence and Transmembrane Helices (2640 entries)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown by sitting-drop vapor diffusion at room temperature in 200 mM NaBr, 2.2 M (NH4)2SO4, at a protein:mother liquor ratio of 70:30 and an AbLpxM concentration of 21 mg/ml
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
lipid A in lipopolysaccharide (LPS) of Escherichia coli mutant strains is modified by the introduction of myristoyltransferase gene cloned from Klebsiella pneumoniae. When the lpxL2 gene is introduced into the mutant having lipid A containing only 3-hydroxymyristic acids, it produces lipid A with two additional myristic acids (C14:0). When the same gene is introduced into the mutant with pentaacylated lipid A containing one lauric acid (C12:0), C12:0 is replaced by C14:0
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
mutants deleted either for the Braun lipoprotein genes lppA and lppB or in combination with the msbB gene, which encodes an acetyltransferase required for lipid A modification of lipopolysaccharide provided complete protection to immunized mice against a lethal oral challenge dose of wild type Salmonella typhimurium. These mutants may serve as excellent vaccine candidates and also provide a platform for delivering heterologous antigens
drug development
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mutants deleted either for the Braun lipoprotein genes lppA and lppB or in combination with the msbB gene, which encodes an acetyltransferase required for lipid A modification of lipopolysaccharide provided complete protection to immunized mice against a lethal oral challenge dose of wild type Salmonella typhimurium. These mutants may serve as excellent vaccine candidates and also provide a platform for delivering heterologous antigens
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Clementz, T.; Zhou, Z.; Raetz, C.R.
Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate incorporation by HtrB
J. Biol. Chem.
272
10353-10360
1997
Escherichia coli (P24205)
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 (A7MEA8), Cronobacter sakazakii, Cronobacter sakazakii ATCC BAA-894 (A7MEA8)
brenda
Korneev, K.V.; Kondakova, A.N.; Arbatsky, N.P.; Novototskaya-Vlasova, K.A.; Rivkina, E.M.; Anisimov, A.P.; Kruglov, A.A.; Kuprash, D.V.; Nedospasov, S.A.; Knirel, Y.A.; Drutskaya, M.S.
Distinct biological activity of lipopolysaccharides with different lipid A acylation status from mutant strains of Yersinia pestis and some members of genus Psychrobacter
Biochemistry (Moscow)
79
1333-1338
2014
Yersinia pestis, Yersinia pestis KM260
brenda
Rubin, E.J.; OBrien, J.P.; Ivanov, P.L.; Brodbelt, J.S.; Trent, M.S.
Identification of a broad family of lipid A late acyltransferases with non-canonical substrate specificity
Mol. Microbiol.
91
887-899
2014
Helicobacter pylori (Q9ZMG5), Helicobacter pylori
brenda
Xu, H.; Ling, J.; Gao, Q.; He, H.; Mu, X.; Yan, Z.; Gao, S.; Liu, X.
Role of the lpxM lipid A biosynthesis pathway gene in pathogenicity of avian pathogenic Escherichia coli strain E058 in a chicken infection model
Vet. Microbiol.
166
516-526
2013
Escherichia coli, Escherichia coli E058
brenda
Erova, T.; Kirtley, M.; Fitts, E.; Ponnusamy, D.; Baze, W.; Andersson, J.; Cong, Y.; Tiner, B.; Sha, J.; Chopra, A.
Protective immunity elicited by oral immunization of mice with Salmonella enterica serovar typhimurium braun lipoprotein (Lpp) and acetyltransferase (MsbB) mutants
Front. Cell. Infect. Microbiol.
6
148
2016
Salmonella enterica subsp. enterica serovar Typhimurium (A0A0F6B2L6), Salmonella enterica subsp. enterica serovar Typhimurium 14028s (A0A0F6B2L6)
brenda
Taniguchi, C.; Sugawara, T.; Onoue, S.; Kawahara, K.
Structural modification of Escherichia coli lipid A by myristoyltransferase gene from Klebsiella pneumoniae
Microbiol. Immunol.
63
334-337
2019
Klebsiella pneumoniae, Klebsiella pneumoniae NBRC 14940T
brenda
Fathy Mohamed, Y.; Hamad, M.; Ortega, X.; Valvano, M.
The LpxL acyltransferase is required for normal growth and penta-acylation of lipid A in Burkholderia cenocepacia
Mol. Microbiol.
104
144-162
2017
Burkholderia cenocepacia (B4E7Z9), Burkholderia cenocepacia ATCC BAA-245 (B4E7Z9)
brenda
Dovala, D.; Rath, C.; Hu, Q.; Sawyer, W.; Shia, S.; Elling, R.; Knapp, M.; Metzger, L.I.
Structure-guided enzymology of the lipid a acyltransferase LpxM reveals a dual activity mechanism
Proc. Natl. Acad. Sci. USA
113
E6064-E6071
2016
Acinetobacter baumannii (A0A1Y1P7X1)
brenda
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Release 2023.1 (January 2023)
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