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Information on EC 2.7.8.24 - phosphatidylcholine synthase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HXE9

for references in articles please use BRENDA:EC2.7.8.24
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IUBMB Comments
Requires divalent cations, with Mn2+ being more effective than Mg2+.
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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9HXE9
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
pc synthase, phosphatidylcholine synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CDP-diglyceride-choline O-phosphatidyltransferase
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CDPdiglyceride-choline O-phosphatidyltransferase
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PC synthase
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phosphatidylcholine synthase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
CDP-diacylglycerol:choline O-phosphatidyltransferase
Requires divalent cations, with Mn2+ being more effective than Mg2+.
CAS REGISTRY NUMBER
COMMENTARY hide
243666-86-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CDP-diacylglycerol + choline
CMP + phosphatidylcholine
show the reaction diagram
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-
?
CDP-diacylglycerol + choline
CMP + phosphatidylcholine
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CDP-diacylglycerol + choline
CMP + phosphatidylcholine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
requires the presence of bivalent cations such as Mg2+ or Mn2+ for its function, with Mn2+ being much more efficient (more than 20fold higher activity) than Mg2+
Mn2+
requires the presence of bivalent cations such as Mg2+ or Mn2+ for its function, with Mn2+ being much more efficient (more than 20fold higher activity) than Mg2+. At 10 mM Mn2+ maximal activity is reached
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
an integral membrane protein
Manually annotated by BRENDA team
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
the presence of Triton X-100 is required in order to detect enzyme activity. 0.2% (w/v) Triton X-100 gives maximal enzyme activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wilderman, P.J.; Vasil, A.I.; Martin, W.E.; Murphy, R.C.; Vasil, M.L.
Pseudomonas aeruginosa synthesizes phosphatidylcholine by use of the phosphatidylcholine synthase pathway
J. Bacteriol.
184
4792-4799
2002
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Martinez-Morales, F.; Schobert, M.; Lopez-Lara, I.M.; Geiger, O.
Pathways for phosphatidylcholine biosynthesis in bacteria
Microbiology
149
3461-3471
2003
Agrobacterium tumefaciens, Borreliella burgdorferi, Bradyrhizobium japonicum, Brucella melitensis (D0B707), Brucella melitensis, Legionella pneumophila, Mesorhizobium loti, Pseudomonas aeruginosa, Rhizobium leguminosarum, Sinorhizobium meliloti
Manually annotated by BRENDA team
Geiger, O.; Lopez-Lara, I.M.; Sohlenkamp, C.
Phosphatidylcholine biosynthesis and function in bacteria
Biochim. Biophys. Acta
1831
503-513
2013
Agrobacterium tumefaciens, Bacillus subtilis, Brucella abortus, Brucella melitensis, Escherichia coli, Pseudomonas aeruginosa (Q9HXE9), Pseudomonas putida, Pseudomonas putida KT 2240, Sinorhizobium meliloti
Manually annotated by BRENDA team