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Information on EC 2.7.8.42 - Kdo2-lipid A phosphoethanolamine 7''-transferase and Organism(s) Escherichia coli and UniProt Accession P37661

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IUBMB Comments
The enzyme has been characterized from the bacterium Escherichia coli. It is activated by Ca2+ ions and is silenced by the sRNA MgrR.
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Escherichia coli
UNIPROT: P37661
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
eptB, lipid A phosphoethanolamine transferase, phosphoethanolamine transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoethanolamine transferase
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eptB
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
diacylphosphatidylethanolamine:alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid-A 7''-phosphoethanolaminetransferase
The enzyme has been characterized from the bacterium Escherichia coli. It is activated by Ca2+ ions and is silenced by the sRNA MgrR.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diacylphosphatidylethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
show the reaction diagram
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in the presence of Ca2+, enzyme transfers the phosphatidylethanolamine group. Stoichiometric amounts of diacylglycerol are generated during the transfer to Kdo2-lipid A
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?
diacylphosphatidylethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid IVA
diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid IVA
show the reaction diagram
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the phosphoethanolamine substituent is located on the outer Kdo moiety
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
Hfq-dependent small RNA MgrR negatively regulates expression of EptB. Envelope stress response protein Sigma E has positively regulates EptB. The effects of Sigma E and deletion of MgrR on levels of EptB mRNA are independent, and the same 5' end is found in both cases. Sigma E acts directly at the level of transcription initiation for EptB, from the same start point as Sigma 70. When Sigma E is active, synthesis of EptB transcript may outstrip MgrR-dependent degradation. A second sRNA, ArcZ, also directly and negatively regulates EptB
physiological function
a gene replacement mutant is hypersensitive to CaCl2 at 5 mM or higher
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Hfq-dependent small RNA MgrR negatively regulates expression of EptB. Envelope stress response protein Sigma E has positively regulates EptB. The effects of Sigma E and deletion of MgrR on levels of EptB mRNA are independent, and the same 5? end is found in both cases. Sigma E acts directly at the level of transcription initiation for EptB, from the same start point as Sigma 70. When Sigma E is active, synthesis of EptB transcript may outstrip MgrR-dependent degradation. A second sRNA, ArcZ, also directly and negatively regulates EptB
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
276
1156-1163
2001
Escherichia coli (P37661)
Manually annotated by BRENDA team
Reynolds, C.M.; Kalb, S.R.; Cotter, R.J.; Raetz, C.R.
A phosphoethanolamine transferase specific for the outer 3-deoxy-D-manno-octulosonic acid residue of Escherichia coli lipopolysaccharide. Identification of the eptB gene and Ca2+ hypersensitivity of an eptB deletion mutant
J. Biol. Chem.
280
21202-21211
2005
Escherichia coli (P37661)
Manually annotated by BRENDA team
Moon, K.; Six, D.A.; Lee, H.J.; Raetz, C.R.; Gottesman, S.
Complex transcriptional and post-transcriptional regulation of an enzyme for lipopolysaccharide modification
Mol. Microbiol.
89
52-64
2013
Escherichia coli (P37661)
Manually annotated by BRENDA team