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Information on EC 2.4.1.182 - lipid-A-disaccharide synthase and Organism(s) Escherichia coli and UniProt Accession P10441
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EC Tree
2.4.1.182 lipid-A-disaccharide synthaseIUBMB Comments
Involved with EC 2.3.1.129 (acyl-[acyl-carrier-protein]---UDP-N-acetylglucosamine O-acyltransferase) and EC 2.7.1.130 (tetraacyldisaccharide 4'-kinase) in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria.
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Word Map
- 2.4.1.182
- acyltransferase
-
raetz
-
clockwise
- udp-glcnac
- lipopolysaccharide
- paralogue
- lps
- udp-2,3-diacylglucosamine
- castellanii
-
cotranscribed
-
amoebae
-
micelle
- pneumophila
-
bacteriol
-
acanthamoeba
- glycerophospholipids
- resin
- udp-n-acetylglucosamine
- synthesis
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
+
=
+
a lipid A disaccharide
Synonyms
lipid a disaccharide synthase, lcsc/lpxb1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
lipid A disaccharide synthase
synthase, lipid A disaccharide
-
-
-
-
lipid A disaccharide synthase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + a lipid X = UDP + a lipid A disaccharide
enzyme LpxB catalyzes the nucleophilic attack of the 6'-hydroxyl of lipid X (1) on the anomeric carbon of UDP-DAG (2) with UDP as the leaving group. As for other inverting GT-B enzymes, this reaction is thought to proceed by an SN2 mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine:2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine 1-phosphate 2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosaminyltransferase
Involved with EC 2.3.1.129 (acyl-[acyl-carrier-protein]---UDP-N-acetylglucosamine O-acyltransferase) and EC 2.7.1.130 (tetraacyldisaccharide 4'-kinase) in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria.
CAS REGISTRY NUMBER
COMMENTARY
105843-81-0
-
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
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP-2,3-diacylglucosamine + 2,3-diacylglucosamine 1-phosphate
2',3'-diacylglucosamine-(beta,1'-6)-2,3-diacylglucosamine 1-phosphate + UDP
-
-
-
-
?
UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 3-((R)-3-hydroxytetradecanoyl)-N-acetyl-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
0.44% of the activity with UDP-2,3-diacylglucosamine
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
-
-
-
-
?
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
-
-
?
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
-
-
-
?
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
-
-
ir
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
-
-
ir
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
-
product analysis
?
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
2,3-diacylglucosamine 1-phosphate is lipid X
-
?
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
2,3-diacylglucosamine 1-phosphate is lipid X
-
?
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
2,3-diacylglucosamine 1-phosphate is lipid X
-
ir
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
strong preference for 2,3-diacylated substrates, but the (R)-3-hydroxy substituent is not required
-
ir
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
involved with EC 2.3.1.129 and EC 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of E. coli and other gram-negative bacteria
-
-
?
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
involved in lipid A biosynthesis
-
-
?
additional information
?
-
LpxB combines lipid X with the preceding lipid metabolite, UDP-2,3-bis(beta-hydroxymyristoyl)-D-glucosamine, to form lipid A disaccharide
-
-
?
additional information
?
-
LpxB only consumes lipid X in a 1:1 ratio with UDP-2,3-bis(beta-hydroxymyristoyl)-D-glucosamine. Near irreversibility of the LpxB enzyme
-
-
?
additional information
?
-
analysis of UDP binding site structure and ligand-bound structure of LpxB. The GlcNAc moiety is highly flexible or that UDP-GlcNAc is hydrolysed during soaking. The uracil base binds in a hydrophobic pocket formed by L197, P198, P231, and V233, which is on the second Rossmann-fold domain and facing the deep inter-domain cleft. The P231 carbonyl oxygen also hydrogen-bonds with N3 of uracil and the G199 amide nitrogen hydrogen-bonds with the O4 carbonyl of uracil. In addition, two water molecules connect active site residues to uracil: the first water connects the G199 carbonyl oxygen and the V233 amide nitrogen to O4 of uracil, and the second water connects the G261 amide nitrogen to the O2 carbonyl of uracil
-
-
-
additional information
?
-
-
analysis of UDP binding site structure and ligand-bound structure of LpxB. The GlcNAc moiety is highly flexible or that UDP-GlcNAc is hydrolysed during soaking. The uracil base binds in a hydrophobic pocket formed by L197, P198, P231, and V233, which is on the second Rossmann-fold domain and facing the deep inter-domain cleft. The P231 carbonyl oxygen also hydrogen-bonds with N3 of uracil and the G199 amide nitrogen hydrogen-bonds with the O4 carbonyl of uracil. In addition, two water molecules connect active site residues to uracil: the first water connects the G199 carbonyl oxygen and the V233 amide nitrogen to O4 of uracil, and the second water connects the G261 amide nitrogen to the O2 carbonyl of uracil
-
-
-
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
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
additional information
?
-
LpxB combines lipid X with the preceding lipid metabolite, UDP-2,3-bis(beta-hydroxymyristoyl)-D-glucosamine, to form lipid A disaccharide
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate
-
-
-
-
?
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
-
-
-
?
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
involved with EC 2.3.1.129 and EC 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of E. coli and other gram-negative bacteria
-
-
?
UDP-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
UDP + 2,3-bis((R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2,3-bis((R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate
-
involved in lipid A biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
the ability of LpxB6S to catalyze the reaction of Triton X-100-solubilized substrates is completely abolished
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
-
between 0 and 0.5 mM Triton X-100 increases the apparent specific activity 5fold
additional information
LpxB catalysis requires the presence of detergents
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
bi-substrate Michaelis-Menten kinetics for enzyme LpxB, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
LpxB activity is dependent upon the bulk surface concentration of ist substrates in a mixed micelle assay system, suggesting that catalysis occurs at the membrane interface
additional information
-
enzyme possibly interacts with membranes due to its extreme hydrophobic reaction product
-
membrane-associated. LpxB is a membrane surface active enzyme. The hydrophobic patch (V66, V68, L69, L72, L75, and L76) is essential for productive membrane association or substrate binding
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
LpxB is among the most highly conserved enzymes in the Raetz pathway
evolution
LpxB is an inverting glycosyltransferase of family 19 of the GT-B superfamily
metabolism
the enzyme is involved in the lipid A biosynthesis catalyzing the fifth step, LpxH and LpxB may form a complex that performs metabolic channeling. LpxB combines lipid X with the preceding lipid metabolite, UDP-2,3-bis(beta-hydroxymyristoyl)-D-glucosamine, to form lipid A disaccharide. Development of a quantitative model of the nine enzyme-catalyzed steps of Escherichia coli lipid A biosynthesis, modelling, detailed overview
metabolism
LpxB is a glycosyltransferase in the Raetz (lipid A synthesis) pathway that catalyzes nucleophilic attack of the 6'-hydroxyl of lipid X on the anomeric carbon of UDP-diacyl-glucosamine (UDP-DAG) to form beta(1-6)-tetraacyl-disaccharide 1-phosphate (lipid A disaccharide)
physiological function
most Gram-negative bacteria are surrounded by a glycolipid called lipopolysaccharide (LPS), which forms a barrier to hydrophobic toxins and, in pathogenic bacteria, is a virulence factor. During LPS biosynthesis, the membrane-associated glycosyltransferase (LpxB) forms a tetraacylated disaccharide that is further acylated to form the membrane anchor moiety of LPS. LpxB is essential for growth of Escherichia coli and is among the most highly conserved enzymes in the Raetz pathway
physiological function
role of LpxB as the disaccharide synthetase to condense UDP-DAGn with lipid X to form DSMP and UDP
additional information
Escherichia coli enzyme LpxB has a glycosyltransferase-B family fold but with a highly intertwined, C-terminally swapped dimer comprising four domains. Homology modeling using the UDP-N-acetylglucosamine 2-epimerase structure from Thermus thermophilus strain HB8 (PDB ID 1V4V) as template, structure comparisons, overview. The hydrophobic patch (V66, V68, L69, L72, L75, and L76) is essential for productive membrane association or substrate binding
additional information
-
Escherichia coli enzyme LpxB has a glycosyltransferase-B family fold but with a highly intertwined, C-terminally swapped dimer comprising four domains. Homology modeling using the UDP-N-acetylglucosamine 2-epimerase structure from Thermus thermophilus strain HB8 (PDB ID 1V4V) as template, structure comparisons, overview. The hydrophobic patch (V66, V68, L69, L72, L75, and L76) is essential for productive membrane association or substrate binding
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
78900
dimeric soluble recombinant enzyme, analytical ultracentrifugation
42000
additional information
additional information
-
glycerol-3-phosphate dehydrogenase specifically binds to purified His-tagged enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
purified recombinant LpxB tends to form large, soluble aggregates
additional information
-
purified recombinant LpxB tends to form large, soluble aggregates
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified soluble recombinant enzymes, LpxB in the apo form and bound to UDP: LpxB7S, SeMet-LpxB7S, LpxB7S with UDP, and mutant LpxB6S (V66S/V68S/L69S/L72S/L75S/L76S), the ligand-bound structure of LpxB is obtained by soaking crystals with 10mM UDP-N-acytlglucosamine (UDP-GlcNAc), X-ray diffraction structure determination and analysis at 1.98-3.43 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F298E/N316A
site-directed mutagenesis, mutant LpxBFN, the mutant shows 0.0078% of wild-type activity
L69S
site-directed mutagenesis, the mutation improves solubility and yield of LpxB
L72S
site-directed mutagenesis, the mutation improves solubility and yield of LpxB
L72S/L75S
site-directed mutagenesis, the mutant shows 1.74% of wild-type enzyme activity
L72S/L75S/L76S
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
L72S/L76S
site-directed mutagenesis, the mutant shows 32.2% of wild-type enzyme activity
L75S
site-directed mutagenesis, the mutation improves solubility and yield of LpxB
L75S/L76S
site-directed mutagenesis, the mutant shows 30.6% of wild-type enzyme activity
L76S
site-directed mutagenesis, the mutation improves solubility and yield of LpxB
M207S
site-directed mutagenesis, structure determination as selenomethionine-labeled enzyme
N316A
site-directed mutagenesis, mutant LpxBFN, the mutant shows 0.34% of wild-type activity
R201A
site-directed mutagenesis, mutant LpxBFN, the mutant shows 0.0051% of wild-type activity
V66S
site-directed mutagenesis, the mutation improves solubility and yield of LpxB
V66S/V68S/L69S
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
V66S/V68S/L69S/L72S/L75S/L76S
site-directed mutagenesis, mutant LpxB6S , the mutation improves solubility and yield of LpxB and shows the least aggregation of all mutants on a size exclusion column
V68S
site-directed mutagenesis, the mutation improves solubility and yield of LpxB
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification as recombinant His-tagged protein from overproducing strain in presence of Triton X-100, copurification of glycerol-3-phosphate dehydrogenase specifically bound to the enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene lpxB, recombinant expression of His6-tagged wild-type and mutant enzymes, coexpression of His6-tagged mutants LpxBR201A, LpxBN316A, and LpxBFN, and pull-down assays
expression from plasmid, DNA sequence analysis, lpxB gene is cotranscribed with the lpxA gene located in the same operon
-
overexpression in Escherichia coli from plasmid, alone and together with gene lpxA, UDP-GlcNAc acyltransferase
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
synthesis of a variety of artificial fluorinated lipid A precursor analogues on a preparative scale for investigation of structure-function relationships of lipid A derivatives
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ray, B.L.; Painter, G.; Raetz, C.R.H.
The biosynthesis of gram-negative endotoxin. Formation of lipid A disaccharides from monosaccharide precursors in extracts of Escherichia coli
J. Biol. Chem.
259
4852-4859
1984
Escherichia coli
Crowell, D.N.; Reznikoff, W.S.; Raetz, C.R.H.
Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide synthase
J. Bacteriol.
169
5727-5734
1987
Escherichia coli
Crowell, D.N.; Anderson, M.S.; Raetz, C.R.H.
Molecular cloning of the genes for lipid A disaccharide synthase and UDP-N-acetylglucosamine acyltransferase in Escherichia coli
J. Bacteriol.
168
152-159
1986
Escherichia coli
Radika, K.; Raetz, C.R.H.
Purification and properties of lipid A disaccharide synthase of Escherichia coli
J. Biol. Chem.
263
14859-14867
1988
Escherichia coli, Escherichia coli MC1061/pSR8
Raetz, C.R.H.
Lipid A disaccharide synthase from Escherichia coli
Methods Enzymol.
209
455-466
1992
Escherichia coli, Escherichia coli MC1061/pSR8
Vyplel, H.; Scholz, D.; Loibner, H.; Kern, M.; Bednarik, K.; Schaller, H.
Synthesis of fluorinated analogues of lipid A
Tetrahedron Lett.
33
1261-1264
1992
Escherichia coli
-
Milla, M.E.; Raetz, C.R.H.
Association of lipid A disaccharide synthase with aerobic glycerol-3-phosphate dehydrogenase in extracts of Escherichia coli
Biochim. Biophys. Acta
1304
245-253
1996
Escherichia coli
Metzger, L.E.; Raetz, C.R.
Purification and characterization of the lipid A disaccharide synthase (LpxB) from Escherichia coli, a peripheral membrane protein
Biochemistry
48
11559-11571
2009
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Escherichia coli (P10441)
Zhou, P.; Zhao, J.
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Chlamydia trachomatis (O84416), Chlamydia trachomatis D/UW-3/Cx (O84416), Escherichia coli (P10441)
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