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show all sequences of 2.7.8.30

Phosphoethanolamine transferase LptA in Haemophilus ducreyi modifies lipid A and contributes to human defensin resistance in vitro

Trombley, M.P.; Post, D.M.; Rinker, S.D.; Reinders, L.M.; Fortney, K.R.; Zwickl, B.W.; Janowicz, D.M.; Baye, F.M.; Katz, B.P.; Spinola, S.M.; Bauer, M.E.; PLoS ONE 10, e0124373 (2015)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Haemophilus ducreyi
G1UBA2
-
-
Haemophilus ducreyi 35000HP
G1UBA2
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylphosphatidylethanolamine + lipid A
-
735018
Haemophilus ducreyi
diacylglycerol + lipid A 1-(2-aminoethyl phosphate)
LptA confers the phosphatidylethanolamine modification to lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
-
735018
Haemophilus ducreyi 35000HP
diacylglycerol + lipid A 1-(2-aminoethyl phosphate)
LptA confers the phosphatidylethanolamine modification to lipid A
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylphosphatidylethanolamine + lipid A
-
735018
Haemophilus ducreyi
diacylglycerol + lipid A 1-(2-aminoethyl phosphate)
LptA confers the phosphatidylethanolamine modification to lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
-
735018
Haemophilus ducreyi 35000HP
diacylglycerol + lipid A 1-(2-aminoethyl phosphate)
LptA confers the phosphatidylethanolamine modification to lipid A
-
-
?
General Information
General Information
Commentary
Organism
physiological function
generation of mutants defective in all three putative phosphoethanolamine transferase genes LptA, PtdA, and PtdB. The triple mutant is significantly more susceptible to both alpha- and beta-defensins. Complementation of all three genes restores parental levels of antimicrobial peptide resistance. Deletion of all three phosphoethanolamine transferase genes results in a significant increase in the negativity of the mutant cell surface. LptA is required for phosphoethanolamine modification of lipid A; PtdA and PtdB do not affect phosphoethanolamine modification of lipooligosaccharide. In human inoculation experiments, the triple mutant is as virulent as its parent strain
Haemophilus ducreyi
General Information (protein specific)
General Information
Commentary
Organism
physiological function
generation of mutants defective in all three putative phosphoethanolamine transferase genes LptA, PtdA, and PtdB. The triple mutant is significantly more susceptible to both alpha- and beta-defensins. Complementation of all three genes restores parental levels of antimicrobial peptide resistance. Deletion of all three phosphoethanolamine transferase genes results in a significant increase in the negativity of the mutant cell surface. LptA is required for phosphoethanolamine modification of lipid A; PtdA and PtdB do not affect phosphoethanolamine modification of lipooligosaccharide. In human inoculation experiments, the triple mutant is as virulent as its parent strain
Haemophilus ducreyi
Other publictions for EC 2.7.8.30
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)
735018
Trombley
Phosphoethanolamine transferas ...
Haemophilus ducreyi, Haemophilus ducreyi 35000HP
PLoS ONE
10
e0124373
2015
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1
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739106
Nowicki
Extracellular zinc induces pho ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14
Mol. Microbiol.
97
166-178
2015
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739495
Piek
The role of oxidoreductases in ...
Neisseria sp.
PLoS ONE
9
e106513
2014
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734476
Wanty
The structure of the neisseria ...
Neisseria meningitidis, Neisseria meningitidis MC58
J. Mol. Biol.
425
3389-3402
2013
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