Information on EC 2.4.1.182 - lipid-A-disaccharide synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.4.1.182
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RECOMMENDED NAME
GeneOntology No.
lipid-A-disaccharide synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
lipid A biosynthesis
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lipid IVA biosynthesis
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Lipopolysaccharide biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine:2,3-bis-(3-hydroxytetradecanoyl)-beta-D-glucosaminyl-1-phosphate 2,3-bis(3-hydroxytetradecanoyl)-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 Escherichia coli.
CAS REGISTRY NUMBER
COMMENTARY hide
105843-81-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
strain C41(DE3)
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Manually annotated by BRENDA team
Escherichia coli MC1061/pSR8
MC1061/pSR8, overvproducing strain
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Manually annotated by BRENDA team
biovars phaseoli CE3 and viciae 8401
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate
UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(1->6)-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate
show the reaction diagram
UDP-2,3-diacylglucosamine + 2,3-diacylglucosamine 1-phosphate
2',3'-diacylglucosamine-(beta,1'-6)-2,3-diacylglucosamine 1-phosphate + UDP
show the reaction diagram
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
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate
UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(1->6)-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement for divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
octyl-beta-D-glucoside
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triton X-100
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between 0 and 0.5 mM Triton X-100 increases the apparent specific activity 5fold
additional information
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no requirement for detergent
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27
2,3-diacylglucosamine 1-phosphate
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0.11
UDP-2,3-diacylglucosamine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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purified enzyme
15.9
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purified enzyme
45
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enzyme from membrane-free lysate, at 30C
183
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after 4.0fold purification, at 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
37
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
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gel filtration
86000
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gel filtration
360000
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gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homooctamer
monomer
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1 * 42000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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30 min, inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, frozen in liquid N2, stable for several years
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
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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
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purification of lpxB-lacZ gene product
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli MN7 (temperature sensitive lpxB mutant), expression of protein complements growth at 30 and 42C; expressed in Escherichia coli MN7 (temperature sensitive lpxB mutant), expression of protein complements growth at 30 and 42C; expressed in Escherichia coli MN7 (temperature sensitive lpxB mutant), expression of protein complements growth at 30 and 42C
expressed in Escherichia coli strain XL1-Blue
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expression from plasmid, DNA sequence analysis, lpxB gene is cotranscribed with the lpxA gene located in the same operon
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overexpression from plasmid as His-tagged protein
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overexpression in Escherichia coli from plasmid, alone and together with gene lpxA, UDP-GlcNAc acyltransferase
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D89A
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mutant shows no residual catalytic activity
R201A
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mutant shows no residual catalytic activity
D89A
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mutant shows no residual catalytic activity
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R201A
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mutant shows no residual catalytic activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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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
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