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Information on EC 2.7.8.8 - CDP-diacylglycerol-serine O-phosphatidyltransferase and Organism(s) Escherichia coli and UniProt Accession P23830

for references in articles please use BRENDA:EC2.7.8.8
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This record set is specific for:
Escherichia coli
UNIPROT: P23830 not found.
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Escherichia coli
Synonyms
archaetidylserine synthase, base-exchange-type -phosphatidylserine synthase, CDP-diacylglycerol:L-serine O-phosphatidyltransferase, CDP-diglyceride-L-serine phosphatidyltransferase, CDP-diglyceride:L-serine phosphatidyltransferase, CDP-diglyceride:serine phosphatidyltransferase, CDPdiacylglycerol-L-serine O-phosphatidyltransferase, CDPdiacylglycerol-serine O-phosphatidyltransferase, CDPdiacylglycerol:L-serine 3-O-phosphatidyltransferase, CDPdiacylglycerol:L-serine O-phosphatidyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
archaetidylserine synthase
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CDP-diacylglycerol:L-serine O-phosphatidyltransferase
CDP-diglyceride-L-serine phosphatidyltransferase
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CDP-diglyceride:L-serine phosphatidyltransferase
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CDP-diglyceride:serine phosphatidyltransferase
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CDPdiacylglycerol-L-serine O-phosphatidyltransferase
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CDPdiacylglycerol-serine O-phosphatidyltransferase
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CDPdiacylglycerol:L-serine 3-O-phosphatidyltransferase
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CDPdiacylglycerol:L-serine O-phosphatidyltransferase
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CDPdiglyceride-serine O-phosphatidyltransferase
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cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:L-serine O-phosphatidyltransferase
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cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:L-serine O-phosphatidyltransferase (CDPdiglyceride)
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phosphatidylserine synthase
phosphatidylserine synthetase
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phosphatidyltransferase, cytidine diphosphoglyceride-serine O-
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PS synthase
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PtdSer synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CDP-diacylglycerol + L-serine = CMP + (3-sn-phosphatidyl)-L-serine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transphosphatidylation
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substituted phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
CDP-diacylglycerol:L-serine 3-sn-phosphatidyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9068-48-8
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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 + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
show the reaction diagram
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-
-
?
CDP-1,2-bis-O-(oleoyl)-sn-glycerol + L-serine
CMP + 1,2-bis-O-(oleoyl)-sn-glycero-3-phospho-L-serine
show the reaction diagram
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41% of the activity compared to CDP-1,2-diacylglycerol with fatty acids from lecithin
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-
?
CDP-1,2-diacylglycerol + L-serine
CMP + 1,2-diacyl-sn-glycerol-3-phospho-L-serine
show the reaction diagram
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fatty acids from lecithin
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-
?
CDP-1,2-dicaproyl-DL-glycerol + L-Ser
CMP + 3-O-sn-1,2-dicaproylphosphatidylserine
show the reaction diagram
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-
-
-
?
CDP-1,2-dipalmitoyl-L-glycerol + L-Ser
CMP + 1,2-dipalmitoylphosphatidylserine
show the reaction diagram
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-
-
-
?
CDP-2,3-bis-O-(oleoyl)-sn-glycerol + L-serine
CMP + 2,3-bis-O-(oleoyl)-sn-glycero-1-phospho-L-serine
show the reaction diagram
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17% of the activity compared to CDP-1,2-diacylglycerol with fatty acids from lecithin
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-
?
CDP-diacylglycerol + glycerol
CMP + phosphatidylglycerol
show the reaction diagram
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low activity
-
?
CDP-diacylglycerol + H2O
CMP + phosphatidic acid
show the reaction diagram
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
show the reaction diagram
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
show the reaction diagram
CDP-diacylglycerol + sn-glycero-3-phosphate
CMP + phosphatidylglycerophosphate
show the reaction diagram
phosphatidylserine + H2O
?
show the reaction diagram
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?
additional information
?
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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 + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
show the reaction diagram
P23830
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-
-
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triton X-100
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inhibits activity as the molar ratio of Triton X-100 to CDP-diacylglycerol raises beyond the point of maximal activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cardiolipin
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activates. The enzyme is completely desensitized by treatment for 5 min at 40°C against the effect of cadiolipin without loss of activity
diphosphatidylglycerol
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membrane association and activity of PtdSer synthase is increased, studied with mixed micelles containing phosphatidylglycerol (one charge) or diphosphatidylglycerol (two charges), the two main anionic membrane lipids in Escherichia coli
phosphatidylethanolamine
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slightly activates. The enzyme is completely desensitized by treatment for 5 min at 40°C against the effect of phosphatidylethanolamine without loss of activity
phosphatidylglycerol
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membrane association and activity of PtdSer synthase is increased, studied with mixed micelles containing phosphatidylglycerol (one charge) or diphosphatidylglycerol (two charges), the two main anionic membrane lipids in Escherichia coli
Triton X-100
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.085
L-Ser
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pH 7.2, 37°C, membrane-bound enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.34
extract supernatant
2.62
after ammonium sulfate precipitation
7.86
purification step SP-Sepharose HP
13.62
purification step Sephadex G-75
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
transphosphatidylation
7 - 8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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possible regulatory mechanism: cross-feedback regulatory model which assumes two forms of phosphatidylserine synthase, only molecules bound with acidic phospholipids of the membrane are active in phosphatidylserine synthesis, whereas others in the cytoplasm are latent
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52800
theoretical
53000
determined by SDS-PAGE
52817
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x * 52817, calculation from nucleotide sequence
54000
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x * 54000, SDS-PAGE
500000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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mutants in the pss gene stop growing after 4 to 5 generations at the restruiction temperature 42°C. The enzyme isolated from such mutants is also temperature-labile
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high ionic strength buffers are neceassary to prevent irreversible precipitation and inactivation of the enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for ar least 1 month
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4°C, 25% loss after 1 months
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
after ammonium sulfate precipitation on a SP-Sepharose and a Sephadex G-75 gel column
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
into the vector pBES for expression in Bacillus subtilis DB104
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
phospholipids, especially phosphatidylserine, have many applications in functional food and pharmaceutical industries
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Larson, T.J.; Dowhan, W.
Ribosomal-associated phosphatidylserine synthetase from Escherichia coli: purification by substrate-specific elution from phosphocellulose using cytidine 5-diphospho-1,2-diacyl-sn-glycerol
Biochemistry
15
5212-5218
1976
Escherichia coli
Manually annotated by BRENDA team
Raetz, C.R.H.; Kennedy, E.P.
Partial purification and properties of phosphatidylserine synthetase from Escherichia coli
J. Biol. Chem.
249
5038-5045
1974
Escherichia coli
-
Manually annotated by BRENDA team
Dowhan, W.; Larson, T.
Phosphatidylserine synthase from Escherichia coli
Methods Enzymol.
71
561-571
1981
Escherichia coli
-
Manually annotated by BRENDA team
Dowhan, W.
Phosphatidylserine synthase from Escherichia coli
Methods Enzymol.
209
287-298
1992
Escherichia coli
Manually annotated by BRENDA team
Raetz, C.R.H.; Kennedy, E.P.
The association of phosphatidylserine synthetase with ribosomes in extracts of Escherichia coli
J. Biol. Chem.
247
2008-2014
1972
Escherichia coli
Manually annotated by BRENDA team
Carman, G.M.; Dowhan, W.
Phosphatidylserine synthase from Escherichia coli. The role of Triton X-100 in catalysis
J. Biol. Chem.
254
8391-8397
1979
Escherichia coli
Manually annotated by BRENDA team
Ishinaga, M.; Kato, M.; Kito, M.
Effects of phospholipids on soluble phosphatidylserine synthetase of Escherichia coli
FEBS Lett.
49
201-202
1974
Escherichia coli
Manually annotated by BRENDA team
Raetz, C.R.H.; Carman, G.M.; Dowhan, W.; Jiang, R.T.; Waszkuc, W.; Loffredo, W.; Tsai, M.D.
Phospholipids chiral at phosphorus. Steric course of the reactions catalyzed by phosphatidylserine synthase from Escherichia coli and yeast
Biochemistry
26
4022-4027
1987
Escherichia coli
Manually annotated by BRENDA team
Louie, K.; Chen, Y.C.; Dowhan, W.
Substrate-induced membrane association of phosphatidylserine synthase from Escherichia coli
J. Bacteriol.
165
805-812
1986
Escherichia coli
Manually annotated by BRENDA team
Rilfors, L.; Niemi, A.; Haraldsson, S.; Edwards, K.; Andersson, A.S.; Dowhan, W.
Reconstituted phosphatidylserine synthase from Escherichia coli is activated by anionic phospholipids and micelle-forming amphiphiles
Biochim. Biophys. Acta
1438
281-294
1999
Escherichia coli
Manually annotated by BRENDA team
Matsumoto, K.
Phosphatidylserine synthase from bacteria
Biochim. Biophys. Acta
1348
214-227
1997
Bacillus subtilis, Escherichia coli
Manually annotated by BRENDA team
Linde, K.; Grobner, G.; Rilfors, L.
Lipid dependence and activity control of phosphatidylserine synthase from Escherichia coli
FEBS Lett.
575
77-80
2004
Escherichia coli
Manually annotated by BRENDA team
Morii, H.; Koga, Y.
CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus
J. Bacteriol.
185
1181-1189
2003
Escherichia coli
Manually annotated by BRENDA team
Zhang, Y.N.; Lu, F.P.; Chen, G.Q.; Li, Y.; Wang, J.L.
Expression, purification, and characterization of phosphatidylserine synthase from Escherichia coli K12 in Bacillus subtilis
J. Agric. Food Chem.
57
122-126
2009
Escherichia coli, Escherichia coli (P23830)
Manually annotated by BRENDA team
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