BRENDA - Enzyme Database
show all sequences of 2.7.8.42

Ca2+-induced phosphoethanolamine transfer to the outer 3-deoxy-D-manno-octulosonic acid moiety of Escherichia coli. A novel membrane enzyme dependent upon phosphatidylethanolamine

Kanipes, M.; Lin, S.; Cotter, R.; Raetz, C.; J. Biol. Chem. 276, 1156-1163 (2001)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
membranes from Escherichia coli grown on 5-50 mM CaCl2 contain a phosphoethanolamine transferase that uses the precursor Kdo2-[4*-32P]lipid IVA as an acceptor. Transferase is not present in membranes of Escherichia coli grown with 5 mM MgCl2, BaCl2, or ZnCl2
Escherichia coli
16020
-
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
P37661
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
diacylphosphatidylethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid IVA
-
734135
Escherichia coli
diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid IVA
the phosphoethanolamine substituent is located on the outer Kdo moiety
-
-
?
Synonyms
Synonyms
Commentary
Organism
eptB
-
Escherichia coli
phosphoethanolamine transferase
-
Escherichia coli
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
membranes from Escherichia coli grown on 5-50 mM CaCl2 contain a phosphoethanolamine transferase that uses the precursor Kdo2-[4*-32P]lipid IVA as an acceptor. Transferase is not present in membranes of Escherichia coli grown with 5 mM MgCl2, BaCl2, or ZnCl2
Escherichia coli
16020
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
diacylphosphatidylethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid IVA
-
734135
Escherichia coli
diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid IVA
the phosphoethanolamine substituent is located on the outer Kdo moiety
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Escherichia coli
Expression
Organism
Commentary
Expression
Escherichia coli
membranes from Escherichia coli grown on 5-50 mM CaCl2 contain a phosphoethanolamine transferase that uses the precursor Kdo2-[4*-32P]lipid IVA as an acceptor. Transferase is not present in membranes of Escherichia coli grown with 5 mM MgCl2, BaCl2, or ZnCl2
up
Expression (protein specific)
Organism
Commentary
Expression
Escherichia coli
membranes from Escherichia coli grown on 5-50 mM CaCl2 contain a phosphoethanolamine transferase that uses the precursor Kdo2-[4*-32P]lipid IVA as an acceptor. Transferase is not present in membranes of Escherichia coli grown with 5 mM MgCl2, BaCl2, or ZnCl2
up
Other publictions for EC 2.7.8.42
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
Synonyms
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)
739099
Moon
Complex transcriptional and po ...
Escherichia coli
Mol. Microbiol.
89
52-64
2013
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734192
Cullen
Characterization of unique mod ...
Campylobacter jejuni
J. Biol. Chem.
287
3326-3336
2012
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734149
Reynolds
A phosphoethanolamine transfer ...
Escherichia coli
J. Biol. Chem.
280
21202-21211
2005
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734135
Kanipes
Ca2+-induced phosphoethanolami ...
Escherichia coli
J. Biol. Chem.
276
1156-1163
2001
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