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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
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2.7.8.8 CDP-diacylglycerol-serine O-phosphatidyltransferaseSpecify your search results
Word Map
- 2.7.8.8
- phospholipid
- phosphatidylethanolamine
- phosphatidylcholine
- cardiolipin
- phosphatidylglycerol
- cytidylyltransferase
- phosphatidylglycerophosphate
- cdp-ethanolamine
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ptdetn
-
3-phosphatidyltransferase
-
uasino
- ptdss1
-
phospholipid-synthesizing
- food industry
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
phosphatidylserine synthase, ps synthase, ptdser synthase, phosphatidylserine synthase 1, phosphatidylserine synthetase, ospss-1, cdp-diglyceride:l-serine phosphatidyltransferase, phosphatidylserine synthase1, cdpdiacylglycerol:l-serine o-phosphatidyltransferase, cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:l-serine o-phosphatidyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
archaetidylserine synthase
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CDP-diacylglycerol:L-serine O-phosphatidyltransferase
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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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PSS
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PtdSer synthase
phosphatidylserine synthase
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PtdSer synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CDP-diacylglycerol + L-serine = CMP + (3-sn-phosphatidyl)-L-serine
the enzyme appears to catalyze a ping-pong reaction
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CDP-diacylglycerol + L-serine = CMP + (3-sn-phosphatidyl)-L-serine
two-step ping-pong reaction mechanism involving covalently bound enzyme-phosphatidyl intermediate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
substituted phospho group transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
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-, -
SYSTEMATIC NAME
IUBMB Comments
CDP-diacylglycerol:L-serine 3-sn-phosphatidyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
9068-48-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
-
-
-
?
CDP-1,2-bis-O-(oleoyl)-sn-glycerol + L-serine
CMP + 1,2-bis-O-(oleoyl)-sn-glycero-3-phospho-L-serine
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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
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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
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-
-
-
?
CDP-1,2-dipalmitoyl-L-glycerol + L-Ser
CMP + 1,2-dipalmitoylphosphatidylserine
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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
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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
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low activity
-
?
CDP-diacylglycerol + H2O
CMP + phosphatidic acid
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at 1% of the synthetic rate the enzyme catalyzes the hydrolysis of phosphatidylserine to CMP and phosphatidic acid
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?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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-
-
?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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-
-
?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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-
-
?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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-
-
?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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-
-
?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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-
-
?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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-
-
?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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-
-
?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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equilibrium strongly favors synthesis of phosphatidylserine
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r
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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reaction proceeds with retention of configuration at phosphorus, which suggests a two-step mechanism involving a phosphatidyl-enzyme intermediate
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?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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the enzyme participates in the biosynthesis of phosphatidylethanolamine
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-
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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increase in activity caused by phosphatidylglycerol and diphosphatidylglycerol is physiologically relevant. It may be part of a regulatory mechanism that keeps the balance between phosphatidylethanolamine and the sum of phosphatidylglycerol and diphosphatidylglycerol
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-
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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the enzyme catalyzes the first committed step in the biosynthesis of phosphatidylethanolamine
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-
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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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
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?
CDP-diacylglycerol + sn-glycero-3-phosphate
CMP + phosphatidylglycerophosphate
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?
CDP-diacylglycerol + sn-glycero-3-phosphate
CMP + phosphatidylglycerophosphate
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low activity
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?
additional information
?
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the enzyme also catalyzes the exchange reaction between Ser and phosphatidylserine
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?
additional information
?
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the enzyme also catalyzes the exchange reaction between Ser and phosphatidylserine
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?
additional information
?
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the enzyme also catalyzes the exchange reaction between Ser and phosphatidylserine
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?
additional information
?
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enzyme catalyzes exchange reaction between dCDP-diglyceride and dCDP-diglyceride
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?
additional information
?
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enzyme catalyzes exchange reaction between CMP and CDP-diglyceride
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?
additional information
?
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enzyme catalyzes exchange reaction between CMP and CDP-diglyceride
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?
additional information
?
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enzyme catalyzes exchange reaction between CMP and CDP-diglyceride
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?
additional information
?
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the enzyme is specific for the L-glycerol-3-phosphate isomer of the liponucleotide and does not recognize the D-isomer of the 1-monoacyl derivative
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?
additional information
?
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very low activity with (less than 10% compared to CDP-1,2-diacylglycerol with fatty acids from lecithin): CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol, CDP-1,2-bis-O-(geranylgeranyl)-sn-glycerol, CDP-2,3-bis-O-(phytanyl)-sn-glycerol
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
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-
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?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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the enzyme participates in the biosynthesis of phosphatidylethanolamine
-
-
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
-
increase in activity caused by phosphatidylglycerol and diphosphatidylglycerol is physiologically relevant. It may be part of a regulatory mechanism that keeps the balance between phosphatidylethanolamine and the sum of phosphatidylglycerol and diphosphatidylglycerol
-
-
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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the enzyme catalyzes the first committed step in the biosynthesis of phosphatidylethanolamine
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-
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
-
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
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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
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enzyme is dependent on a nonionic detergent such as Triton X-100
Triton X-100
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dependent on nonionic detergent, at 0.1 mM CDP-diacylglycerol optimal activity occurs at a Triton to substrate molar ratio of 8:1
Triton X-100
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increasing levels of Triton X-100 at low molecular ratios of Triton X-100 to CDP-diacylglycerol stimulate
additional information
-
optimal activity is dependent on ionic strength, 0.3 or higher
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additional information
-
the enzyme reconstituted with lipid vesicles of various compositions exhibits practically no activity in the absence of a detergent and with the substrate CDP-diacylglycerol present only in the lipid vesicles. Inclusion of octylglucoside in the assay mixture increases the activity 20- to 1000fold, the degree of activation depends on the lipid composition of the vesicles. Inclusion of additional CDP-diacylglycerol in the assay mixture increases the activity 5- to 25-fold. When the fraction of phosphatidylglycerol is increased from 15 to 100 mol% in the vesicles the activity increases 10fold using the assay mixture containing octylglucoside. The highest activities are exhibited with the anionic lipids diphosphatidylglycerol and phosphatidic acid while phosphatidylinositol gives lower activity
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additional information
-
activity of phosphatidylserine synthase depends significantly on the nature and level of the lipids in the matrix, at which the enzyme is operating
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
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
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normal function of the enzyme involves membrane association which is primarily induced by the presence of a membrane-associated substrate
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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
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predominantly associated with. The enzyme is associated with both 50 and 30S subunit
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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expression of Escherichia coli phosphatidylserine synthase PssA in various membrane compartments with distinct membrane topologies in yeast cells lacking phosphatidylserine synthase Cho1. PssA is able to complement loss of Cho1 when targeted to the endoplasmic reticulum, peroxisome, or lipid droplet membranes. Synthesised phosphatidylserine can be converted to phosphatidylethanolamine by Psd1, the mitochondrial phosphatidylserine decarboxylase. PssA which has been integrated into the mitochondrial inner membrane from the matrix side can partially complement the loss of Cho1
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
500000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
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
-
Dowhan, W.; Larson, T.
Phosphatidylserine synthase from Escherichia coli
Methods Enzymol.
71
561-571
1981
Escherichia coli
-
Dowhan, W.
Phosphatidylserine synthase from Escherichia coli
Methods Enzymol.
209
287-298
1992
Escherichia coli
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
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
Ishinaga, M.; Kato, M.; Kito, M.
Effects of phospholipids on soluble phosphatidylserine synthetase of Escherichia coli
FEBS Lett.
49
201-202
1974
Escherichia coli
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
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
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
Matsumoto, K.
Phosphatidylserine synthase from bacteria
Biochim. Biophys. Acta
1348
214-227
1997
Bacillus subtilis, Escherichia coli
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
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
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 (P23830), Escherichia coli
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