BRENDA - Enzyme Database
show all sequences of 2.7.8.43

The structure of the neisserial lipooligosaccharide phosphoethanolamine transferase A (LptA) required for resistance to polymyxin

Wanty, C.; Anandan, A.; Piek, S.; Walshe, J.; Ganguly, J.; Carlson, R.W.; Stubbs, K.A.; Kahler, C.M.; Vrielink, A.; J. Mol. Biol. 425, 3389-3402 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
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
Neisseria meningitidis
Crystallization (Commentary)
Crystallization
Organism
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
Neisseria meningitidis
Engineering
Amino acid exchange
Commentary
Organism
additional information
generation of a soluble enzyme mutant by deletion of the membrane binding structure. The mutant does not confer resistance to polymyxin in transformed Escherichia coli cells, in contrast to the wild-type LptA
Neisseria meningitidis
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
-
Neisseria meningitidis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
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
Neisseria meningitidis
additional information
three bound metal ions (two Zn2+ and a Mg2+) are implicated in catalysis
Neisseria meningitidis
Zn2+
metal ions present in the active site are coordinated to Thr280 and to residues conserved among the family of transferases, interaction of the Zn2+ with the active site, binding site structure, overview. The second Zn2+ ion is coordinated by the side chains of His383, His465, and one of the oxygen atoms of the phosphate group attached to Thr280. In LptA, two types of coordination around the Zn1 are observed depending on the state of Thr280. In the case of non-phosphorylated Thr280, the coordination about Zn1 is tetrahedral with the fourth ligand being the free phosphate group. In contrast, when Thr280 is phosphorylated, a penta-coordinated metal is observed with the hydroxyl oxygen atom of Thr280 and one of the phosphate oxygen atoms each interacting weakly with the metal; required, one Zn2+ ion per enzyme molecule coordinated tetrahedrally by the side chains of Glu240, Asp452, and His453 and the hydroxyl oxygen atom of Thr280, very strong binding to the enzyme, binding structure model
Neisseria meningitidis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
Neisseria meningitidis
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
Neisseria meningitidis
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
Neisseria meningitidis MC58
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
Neisseria meningitidis MC58
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Neisseria meningitidis
-
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Neisseria meningitidis NMB
-
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Neisseria meningitidis
Q7DD94
-
-
Neisseria meningitidis
Q7DDQ9
-
-
Neisseria meningitidis NMB
Q7DDQ9
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
phosphoprotein
phosphorylation of the putative nucleophile, Thr280
Neisseria meningitidis
Purification (Commentary)
Commentary
Organism
recombinant wild-type and selenomethionine-labeled His6-tagged soluble periplasmic domain of the enzyme from Escherichia coli by nickel affinity chromatography
Neisseria meningitidis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A
low activity, addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
734476
Neisseria meningitidis
1,2-dihexanoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A
low activity, addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
734476
Neisseria meningitidis
1,2-dihexanoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
734476
Neisseria meningitidis
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
734476
Neisseria meningitidis MC58
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
734476
Neisseria meningitidis
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
734476
Neisseria meningitidis MC58
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
734476
Neisseria meningitidis
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
734476
Neisseria meningitidis NMB
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
additional information
in Neisseria meningitidis, phosphatidylethanolamine typically has acyl chains of C12 and C14 with the first position being occupied with a saturated chain and the second being unsaturated. The recombinant soluble periplasmic domain of the enzyme is active in an aqueous assay but unable to add phoshoethanolamine to lipid A in Escherichia coli strains, lipid A profiles, overview
734476
Neisseria meningitidis
?
-
-
-
-
additional information
enzyme activity assays on the membrane-deleted LptA are performed using 4-nitrophenyl phosphoethanolamine, p-NPPE, as the substrate analogue, the enzyme is capable of cleaving the phosphoethanolamine portion from the p-NPPE chromogenic substrate
734476
Neisseria meningitidis
?
-
-
-
-
additional information
enzyme activity assays on the membrane-deleted LptA are performed using 4-nitrophenyl phosphoethanolamine, p-NPPE, as the substrate analogue, the enzyme is capable of cleaving the phosphoethanolamine portion from the p-NPPE chromogenic substrate
734476
Neisseria meningitidis NMB
?
-
-
-
-
additional information
in Neisseria meningitidis, phosphatidylethanolamine typically has acyl chains of C12 and C14 with the first position being occupied with a saturated chain and the second being unsaturated. The recombinant soluble periplasmic domain of the enzyme is active in an aqueous assay but unable to add phoshoethanolamine to lipid A in Escherichia coli strains, lipid A profiles, overview
734476
Neisseria meningitidis MC58
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
secondary-structure ribbon representation of the soluble domain of LptA, and modeling of the three-dimensional structure of LptA, overview. Possible formation of five intramolecular disulfide bonds: Cys276-Cys286, Cys327-Cys331, Cys348-Cys353, Cys402-Cys410, and Cys499-Cys540
Neisseria meningitidis
Cloned(Commentary) (protein specific)
Commentary
Organism
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
Neisseria meningitidis
recombinant expression of wild-type and selenomethionine-labeled His6-tagged soluble periplasmic domain of the enzyme in Escherichia coli strains CKEC272 and CKEC580
Neisseria meningitidis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
Neisseria meningitidis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
generation of a soluble enzyme mutant by deletion of the membrane binding structure. The mutant does not confer resistance to polymyxin in transformed Escherichia coli cells, in contrast to the wild-type LptA
Neisseria meningitidis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
-
Neisseria meningitidis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
metal ions present in the active site are coordinated to Thr280 and to residues conserved among the family of transferases
Neisseria meningitidis
Mg2+
required, two Mg2+ ions per enzyme molecule, binding structure model
Neisseria meningitidis
additional information
three bound metal ions (two Zn2+ and a Mg2+) are implicated in catalysis
Neisseria meningitidis
Zn2+
metal ions present in the active site are coordinated to Thr280 and to residues conserved among the family of transferases, interaction of the Zn2+ with the active site, binding site structure, overview. The second Zn2+ ion is coordinated by the side chains of His383, His465, and one of the oxygen atoms of the phosphate group attached to Thr280. In LptA, two types of coordination around the Zn1 are observed depending on the state of Thr280. In the case of non-phosphorylated Thr280, the coordination about Zn1 is tetrahedral with the fourth ligand being the free phosphate group. In contrast, when Thr280 is phosphorylated, a penta-coordinated metal is observed with the hydroxyl oxygen atom of Thr280 and one of the phosphate oxygen atoms each interacting weakly with the metal
Neisseria meningitidis
Zn2+
required, one Zn2+ ion per enzyme molecule coordinated tetrahedrally by the side chains of Glu240, Asp452, and His453 and the hydroxyl oxygen atom of Thr280, very strong binding to the enzyme, binding structure model
Neisseria meningitidis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
Neisseria meningitidis
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
Neisseria meningitidis
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
Neisseria meningitidis MC58
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
Neisseria meningitidis MC58
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Neisseria meningitidis
-
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Neisseria meningitidis NMB
-
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
phosphoprotein
phosphorylation of the putative nucleophile, Thr280
Neisseria meningitidis
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and selenomethionine-labeled His6-tagged soluble periplasmic domain of the enzyme from Escherichia coli by nickel affinity chromatography
Neisseria meningitidis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A
low activity, addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
734476
Neisseria meningitidis
1,2-dihexanoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A
low activity, addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
734476
Neisseria meningitidis
1,2-dihexanoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
734476
Neisseria meningitidis
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
734476
Neisseria meningitidis MC58
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
734476
Neisseria meningitidis
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
734476
Neisseria meningitidis MC58
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
734476
Neisseria meningitidis
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
734476
Neisseria meningitidis NMB
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
additional information
in Neisseria meningitidis, phosphatidylethanolamine typically has acyl chains of C12 and C14 with the first position being occupied with a saturated chain and the second being unsaturated. The recombinant soluble periplasmic domain of the enzyme is active in an aqueous assay but unable to add phoshoethanolamine to lipid A in Escherichia coli strains, lipid A profiles, overview
734476
Neisseria meningitidis
?
-
-
-
-
additional information
enzyme activity assays on the membrane-deleted LptA are performed using 4-nitrophenyl phosphoethanolamine, p-NPPE, as the substrate analogue, the enzyme is capable of cleaving the phosphoethanolamine portion from the p-NPPE chromogenic substrate
734476
Neisseria meningitidis
?
-
-
-
-
additional information
enzyme activity assays on the membrane-deleted LptA are performed using 4-nitrophenyl phosphoethanolamine, p-NPPE, as the substrate analogue, the enzyme is capable of cleaving the phosphoethanolamine portion from the p-NPPE chromogenic substrate
734476
Neisseria meningitidis NMB
?
-
-
-
-
additional information
in Neisseria meningitidis, phosphatidylethanolamine typically has acyl chains of C12 and C14 with the first position being occupied with a saturated chain and the second being unsaturated. The recombinant soluble periplasmic domain of the enzyme is active in an aqueous assay but unable to add phoshoethanolamine to lipid A in Escherichia coli strains, lipid A profiles, overview
734476
Neisseria meningitidis MC58
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
secondary-structure ribbon representation of the soluble domain of LptA, and modeling of the three-dimensional structure of LptA, overview. Possible formation of five intramolecular disulfide bonds: Cys276-Cys286, Cys327-Cys331, Cys348-Cys353, Cys402-Cys410, and Cys499-Cys540
Neisseria meningitidis
General Information
General Information
Commentary
Organism
evolution
ethanolamine transferases are members of the YhjW/YjdB/YijP superfamily
Neisseria meningitidis
additional information
analysis of the three-dimensional structure of the soluble catalytic domain of LptA, active-site residues, structure homology, overview; homology structure modeling of the enzyme, active-site residues and metal binding structures, crystal structure analysis, overview
Neisseria meningitidis
physiological function
the addition of PEA to lipid A by lipid A PEA transferase, LptA, is a major mechanism for resistance to polymyxin in Neisseria meningitidis since this species does not synthesize 4-aminoarabinose. The neisserial lipooligosaccharide phosphoethanolamine transferase A is required for resistance to polymyxin
Neisseria meningitidis
General Information (protein specific)
General Information
Commentary
Organism
evolution
ethanolamine transferases are members of the YhjW/YjdB/YijP superfamily
Neisseria meningitidis
additional information
analysis of the three-dimensional structure of the soluble catalytic domain of LptA, active-site residues, structure homology, overview
Neisseria meningitidis
additional information
homology structure modeling of the enzyme, active-site residues and metal binding structures, crystal structure analysis, overview
Neisseria meningitidis
physiological function
the addition of PEA to lipid A by lipid A PEA transferase, LptA, is a major mechanism for resistance to polymyxin in Neisseria meningitidis since this species does not synthesize 4-aminoarabinose. The neisserial lipooligosaccharide phosphoethanolamine transferase A is required for resistance to polymyxin
Neisseria meningitidis
Other publictions for EC 2.7.8.43
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
750867
Hicks
-
Structural basis for the lipo ...
Escherichia coli
Int. J. Mol. Sci.
19
E2680
2018
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1
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1
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1
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1
1
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1
1
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752134
Schultz
Lipopolysaccharide binding to ...
Escherichia coli
Protein Sci.
26
1517-1523
2017
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1
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14
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1
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1
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14
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1
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1
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1
1
1
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3
3
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738476
Liu
A phosphoethanolamine transfer ...
Cronobacter sakazakii, Cronobacter sakazakii BAA894
J. Appl. Microbiol.
121
1444-1456
2016
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1
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1
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2
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4
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2
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2
2
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733635
Handing
The lipooligosaccharide-modify ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
Cell. Microbiol.
17
910-921
2015
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1
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1
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2
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4
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2
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735018
Trombley
Phosphoethanolamine transferas ...
Haemophilus ducreyi, Haemophilus ducreyi ATCC 700724
PLoS ONE
10
e0124373
2015
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1
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1
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1
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7
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5
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1
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5
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2
3
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739106
Nowicki
Extracellular zinc induces pho ...
Pseudomonas aeruginosa
Mol. Microbiol.
97
166-178
2015
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1
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1
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1
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1
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4
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The role of oxidoreductases in ...
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Resistance to the antimicrobia ...
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Phosphorylation of the lipid A ...
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