Information on EC 2.7.8.43 - lipid A phosphoethanolamine transferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.8.43
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RECOMMENDED NAME
GeneOntology No.
lipid A phosphoethanolamine transferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
diacylphosphatidylethanolamine + lipid A 1-(2-aminoethyl diphosphate) = diacylglycerol + lipid A 1,4'-bis(2-aminoethyl diphosphate)
show the reaction diagram
(3)
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diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
(1)
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diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
(2)
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SYSTEMATIC NAME
IUBMB Comments
diacylphosphatidylethanolamine:lipid-A phosphoethanolaminetransferase
The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-beta-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
diverse colistin sensitive and resistant strains, gene pmrA
E2FGC2
UniProt
Manually annotated by BRENDA team
gene ESA_RS09200, formerly ESA_02008
UniProt
Manually annotated by BRENDA team
gene ESA_RS09200, formerly ESA_02008
UniProt
Manually annotated by BRENDA team
human-passaged variant of class I clinical isolate 35000
UniProt
Manually annotated by BRENDA team
gene Hp0022 or eptA
UniProt
Manually annotated by BRENDA team
Helicobacter pylori ATCC 700392 / 26695
gene Hp0022 or eptA
UniProt
Manually annotated by BRENDA team
gene lptA
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-
Manually annotated by BRENDA team
gene eptA
UniProt
Manually annotated by BRENDA team
serovar Typhimurium, gene pmrA
UniProt
Manually annotated by BRENDA team
a lpxM mutant strain, gene pmrA
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-
Manually annotated by BRENDA team
a colistin-resistant clinical isolate from resistant clinical isolate retrieved from bronchoalveolar lavage of a hospitalised patient
UniProt
Manually annotated by BRENDA team
a colistin-resistant clinical isolate from resistant clinical isolate retrieved from bronchoalveolar lavage of a hospitalised patient
UniProt
Manually annotated by BRENDA team
several different strains
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dihexanoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
low activity, addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
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-
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dihexanoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
low activity, addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
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-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + arbutin
diacylglycerol + ?
show the reaction diagram
arbutin is a substrate for the phosphoethanolamine transferase
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-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
?
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A (2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + O-antigen serotype 4av
diacylglycerol + O-antigen serotype 4av (2-aminoethyl diphosphate)
show the reaction diagram
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the serotype 4av O-antigen has the phosphoethanolamine at position 3 of RhaIII (major) or both RhaII and RhaIII (minor)
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?
diacylphosphatidylethanolamine + O-antigen serotype Xv
diacylglycerol + O-antigen serotype Xv (2-aminoethyl diphosphate)
show the reaction diagram
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the serotype Xv O-antigen has the phosphoethanolamine on RhaII, in serotype Yv, mono- and bisphosphorylated O-units generate a block-copolymeric structure, the former being partially O-acetylated at position 6 of GlcNAc and the latter lacking O-acetylation. The serotype Xv O-antigen has the phosphoethanolamine on RhaII
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?
diacylphosphatidylethanolamine + O-antigen serotype Yv
diacylglycerol + O-antigen serotype Yv 3-(2-aminoethyl diphosphate)
show the reaction diagram
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the serotype Yv O-antigen has the same basic carbohydrate backbone structure as that of the classical serotype Y, but differs in the presence of phosphoethanolamine at position 3 of RhaIII (major) or both RhaII and RhaIII (minor)
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?
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
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
?
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A (2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + O-antigen serotype 4av
diacylglycerol + O-antigen serotype 4av (2-aminoethyl diphosphate)
show the reaction diagram
S4UV19
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the serotype 4av O-antigen has the phosphoethanolamine at position 3 of RhaIII (major) or both RhaII and RhaIII (minor)
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?
diacylphosphatidylethanolamine + O-antigen serotype Xv
diacylglycerol + O-antigen serotype Xv (2-aminoethyl diphosphate)
show the reaction diagram
S4UV19
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the serotype Xv O-antigen has the phosphoethanolamine on RhaII
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?
diacylphosphatidylethanolamine + O-antigen serotype Yv
diacylglycerol + O-antigen serotype Yv 3-(2-aminoethyl diphosphate)
show the reaction diagram
S4UV19
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the serotype Yv O-antigen has the same basic carbohydrate backbone structure as that of the classical serotype Y, but differs in the presence of phosphoethanolamine at position 3 of RhaIII (major) or both RhaII and RhaIII (minor)
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
required, the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+
Mg2+
metal ions present in the active site are coordinated to Thr280 and to residues conserved among the family of transferases; required, two Mg2+ ions per enzyme molecule, binding structure model
additional information
three bound metal ions (two Zn2+ and a Mg2+) are implicated in catalysis
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
LpxT
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polymyxin
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resistance to polymyxin for the enzyme is realized by oxidoreductase DsbA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arbutin
arbutin is also a substrate for phosphoethanolamine transferase stimulating its activity, increasing phosphatidylethanolamine turnover leading to accumulation of diacylglycerol toxic for bacteria
PmrA
te enzyme EptA is activated in a PmrA-dependent manner, overview
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additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
E2FGC2;
colistin resistant strains show higher enzyme expression compared to colistin sensitive strains, enzyme expression analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged wild-type and selenomethionine-labeled enzyme EptC, sitting drop vapour diffusion method, mixing of 0.004 ml of 30 mg/ml protein in 25 mM NaCl, 10 mM HEPES, pH 7.5, with 0.001 ml of precipitant solution containing 200 mM diammonium phosphate, 15% w/v PEG 3350, 22°C, X-ray diffraction structure determination and analysis at 2.40-2.80 A resolution, molecular replacement
purified recombinant His6-tagged soluble catalytic domain of LptA, free and selenomethionine-labeled, or in complex with Zn2+ and a truncated form of substrate 1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine, X-ray diffraction structure determination and analysis at 1.43-1.78 A resolution, molecular replacement. and modeling
recombinant His-tagged membrane-deletion mutant enzyme, mixing of 0.001 ml of 5.2 mg/ml protein in 50 mM HEPES, pH 8.0, 50 mM sodium chloride, with 0.001 ml of crystallization solution containing 23-26% PEG 8000, 100 mM ammonium sulfate, 100 mM HEPES, pH 7.5–8.0, 15 mM n-dodecyl-N,N-dimethylamine-N-oxide, and 200 nl of microseeding solution, 20°C, 3-5 days, method optimization, X-ray diffraction structure determination and analysis at 1.7 A resolution
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
all three neisserial oxidoreductases, including DsbA1, DsbA2 and DsbA3, contribute to resistance to polymyxin
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged membrane-deletion mutant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis
recombinant His-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant His6-tagged enzyme from Escherichi coli strain JCB570 and Neisseria meningitidis by nickel affinity chromatography and ultrafiltration
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recombinant wild-type and selenomethionine-labeled His6-tagged soluble periplasmic domain of the enzyme from Escherichia coli by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene cj0256 or eptC
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gene cj0256, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli K-12 strain W3110/EC01
A0A0E1EWJ6;
gene eptA, construction of a pZE21MCS-1 plasmid-based genomic expression library in Escherichia coli strain TOP10, DNA and amino acid sequence determination and analysis, functional EptA enzyme expression in Escherichia coli strain TOP10
gene eptA, quantitative and semi-quantitative reverse-transcriptase (RT) PCR enzyme expression analysis
gene eptC, recombinant expression of C-terminally Gly6-His8-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression of His-tagged enzyme as selenomethionine-labeled enzyme
gene ESA_RS09200, encodes a phosphoethanolamine transferase that specifically adds a phosphoethanolamine to the 4'-phosphate residue of lipid A, but is not regulated by the PmrA-PmrB system, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain W3110
gene HD_0852 or lptA, homology screening and DNA and amino acid sequence determination and analysis; gene lptA, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli
gene Hp0022, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli NovaBlue(DE3) membranes. method optimization
gene lptA
gene lptA, DNA and amino acid sequence determination and analysis, genotyping in Neisseria, recombinant expression of His6-tagged enzyme in Escherichi coli strain JCB570 and in Neisseria meningitidis from low copy expression vector pCMK1001. In Escherichia coli, the stability and activity of neisserial LptA::Hisx6 is entirely dependent upon the coexpression of the EcDsbA oxidoreductase. Although expression of LptA::Hisx6 and EcDsbA in Escherichia coli results in a 32fold increase in polymyxin resistance, the proportion of lipid A headgroups substituted with PEA rises to 26%
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gene lptA, expression from a a multicopy plasmid in Neisseria meningitidis, construction of an lptA-FLAG epitope-tagged fusion Neisseria meningitidis strain HT1295 from strain H44/76
gene lptA, recombinant expression of wild-type and soluble (membrane-deleted) C-terminally His6-tagged enzyme in Escherichia coli DELTAdsbA mutant strain JCB571 from plasmids pCMK255 and pCMK527, expression of wild-type enzyme confers resistance to polymyxin in Escherichia coli, while expression of the truncated soluble mutant does not; recombinant expression of wild-type and selenomethionine-labeled His6-tagged soluble periplasmic domain of the enzyme in Escherichia coli strains CKEC272 and CKEC580
gene pmrA, genetic organization of the pmrCAB genes, PCR-based expression analysis in colistin sensitive and resistant strains
E2FGC2;
gene pmrA, sequence comparisons with Neisseria meningitidis phosphoethanolamine phosphotransferases lptA, lpt3, and lpt6; gene pmrC
genetic screening identifies gene opgE, DNA and amino acid sequence determination and analysis, genetic organization of opg genes in Escherichia coli, overview. The gene is transformed into competent Escherichia coli cells to give pNF752
recombinant expression of His-tagged membrane-deletion mutant enzyme in Escherichia coli strain BL21(DE3)pLysS
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of EptA (PmrC) is under the control of PmrA/PmrB
no upregulation of pmrA by Fe3+ and Mg2+ in strain ATCC 19606
E2FGC2;
the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+, induction is lost in enzyme mutant strain CH020 (DELTApmrA)
transcription of the enzyme eptAPa is regulated by zinc via the ColRS two-component system. The two-component system response regulator ColR activates eptAPa transcription. Transcription of eptAPa is induced by 2 mM ZnSO4 approximately 21fold
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H358A
site-directed mutagenesis, mutation of a potential zinc binding residue
H440A
site-directed mutagenesis, mutation of a potential zinc binding residue
N308A
site-directed mutagenesis, mutation of a potential zinc binding residue
S309A
site-directed mutagenesis, mutation of a potential zinc binding residue
T266A
site-directed mutagenesis, mutation of a potential zinc binding residue
T266S
site-directed mutagenesis, mutation of a potential zinc binding residue
H358A
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site-directed mutagenesis, mutation of a potential zinc binding residue
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H440A
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site-directed mutagenesis, mutation of a potential zinc binding residue
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N308A
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site-directed mutagenesis, mutation of a potential zinc binding residue
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S309A
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site-directed mutagenesis, mutation of a potential zinc binding residue
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T266S
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site-directed mutagenesis, mutation of a potential zinc binding residue
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additional information