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Literature summary for 2.7.8.42 extracted from

  • Kanipes, M.; Lin, S.; Cotter, R.; Raetz, C.
    Ca2+-induced phosphoethanolamine transfer to the outer 3-deoxy-D-manno-octulosonic acid moiety of Escherichia coli. A novel membrane enzyme dependent upon phosphatidylethanolamine (2001), J. Biol. Chem., 276, 1156-1163.
    View publication on PubMed
Search for more literature for 2.7.8.42

Localization

Localization Comment 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
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Organism

Organism UniProt Comment Textmining
Escherichia coli P37661
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diacylphosphatidylethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid IVA
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 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 Comment Organism
eptB
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 Escherichia coli
phosphoethanolamine transferase
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 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

Expression

Organism Comment 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