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Information on EC 2.7.8.8 - CDP-diacylglycerol-serine O-phosphatidyltransferase
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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
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uasino
- ptdss1
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phospholipid-synthesizing
- food industry
The enzyme appears in viruses and cellular organisms
Synonyms
phosphatidylserine synthase, ps synthase, ptdser synthase, phosphatidylserine synthase 1, phosphatidylserine synthetase, ospss-1, cdp-diglyceride:l-serine phosphatidyltransferase, phosphatidylserine synthase1, ospss, cdp-diacylglycerol-serine o-phosphatidyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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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CHO1
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
phosphatidyltransferase, cytidine diphosphoglyceride-serine O-
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PS synthase
PSS
PSS1
PtdSer synthase
CDP-diacylglycerol:L-serine O-phosphatidyltransferase
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phosphatidylserine synthase
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phosphatidylserine synthetase
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PS synthase
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PSS
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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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CDP-diacylglycerol + L-serine = CMP + (3-sn-phosphatidyl)-L-serine
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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-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-distearoyl-L-glycerol + L-Ser
CMP + 1,2-distearoylphosphatidylserine
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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
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?
CDP-dipalmitoylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
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-
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?
CDP-1,2-dipalmitoyl-L-glycerol + L-Ser
CMP + 1,2-dipalmitoylphosphatidylserine
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?
CDP-1,2-dipalmitoyl-L-glycerol + L-Ser
CMP + 1,2-dipalmitoylphosphatidylserine
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?
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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?
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-sn-phosphatidyl)-L-serine
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?
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
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?
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
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?
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
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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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?
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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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?
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
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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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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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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
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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
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optimal activity is dependent on ionic strength, 0.3 or higher
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additional information
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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
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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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dwarfism
Lenz-Majewski Hyperostotic Dwarfism With Hyperphosphoserinuria From A Novel Mutation In PTDSS1 Encoding Phosphatidylserine Synthase 1.
Hypersensitivity
Envelope composition and antibiotic hypersensitivity of Escherichia coli mutants defective in phosphatidylserine synthetase.
Neoplasms
Distinct Lipidomic Landscapes Associated with Clinical Stages of Urothelial Cancer of the Bladder.
Parkinson Disease
Elevated activity of phospholipid biosynthetic enzymes in substantia nigra of patients with Parkinson's disease.
Starvation
Regulation of CDP-diacylglycerol synthesis and utilization by inositol and choline in Schizosaccharomyces pombe.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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isoform PSS1 promoter activity is prominent in developing anthers
brenda
additional information
isozyme OsPSS-1 gene is expressed predominantly in elongating cells
brenda
additional information
quantitative reverse transcription polymerase chain reaction (qRT-PCR) analyses of wild-type plants reveals that OsPSS-1 is expressed in various organs, including roots, culms, and leaves, with the highest expression in panicles
brenda
additional information
predominantly expressed in elongating cells
brenda
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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
brenda
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isoform PSS1 is localized in endoplasmic reticulum membrane during pollen development
brenda
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isoform PSS1 is localized in nuclei during pollen development
brenda
additional information
OsPSS-1 localizes to organelles associated with exocytosis
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brenda
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normal function of the enzyme involves membrane association which is primarily induced by the presence of a membrane-associated substrate
brenda
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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
brenda
sequence contains contains eight transmembrane domains
brenda
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predominantly associated with. The enzyme is associated with both 50 and 30S subunit
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
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a phosphatidylserine synthase deletion mutant lacks phosphatidylserine, has decreased phosphatidylethanolamine, exhibits defects in cell wall integrity, mitochondrial function, filamentous growth, and is avirulent in a mouse model of systemic candidiasis
malfunction
disruption of PSS1 causes severe dwarfism, smaller lateral organs and reduced size of inflorescence meristem. Both cell division and cell elongation are affected in the pss1-1 mutant. The defect in meristem maintenance is recovered and the expression of WUS and CLV3 are restored in the pss1-1 clv1-1 double mutant. Both shootstemless (STM) and brevipedicellus (BP) are upregulated, and auxin distribution is disrupted in rosette leaves of pss1-1 mutant, expression of BP, which is also a regulator of internode development, is lost in the pss1-1 inflorescence stem. Phenotypes, detailed overview
malfunction
mutation of OsPSS-1 leads to compromised delivery of CESA4 and secGFP towards the cell surface, resulting in weakened intercellular adhesion and disorganized cell arrangement in parenchyma. The Dwarf phenotype of shortened uppermost internode 1 (sui1) is caused by mutations in phosphatidylserine synthase. The phenotype of sui1-4 is caused largely by the reduction in cellulose contents in the whole plant and detrimental delivery of pectins in the uppermost internode. sui1-4 plants exhibit compromised secretion. The mutants show reduced length of both panicles and internodes, especially the uppermost internode, accompanied with reduced fertility, decreased grain size and slightly increased tiller number, defective pectin secretion, detailed overview. A large amount of OsCESA4 remained in the cytoplasm in the mutant, most likely due to failure in delivery to the plasma membrane
physiological function
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phosphatidylserine synthase genes regulate the development of intercalary meristem for internode elongation and also the cell expansion of the panicle stem rachis in rice
physiological function
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phosphatidylserine synthase1 is required for microspore development in Arabidopsis thaliana
physiological function
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the enzyme is essential for cell wall integrity and virulence in Candida albicans
physiological function
phosphatidylserine synthase 1 is required for inflorescence meristem and organ development in Arabidopsis thaliana. Phosphatidylserine, a quantitatively minor membrane phospholipid, is involved in many biological processes besides its role in membrane structure, e.g. it is required for microspore development. Expression of both genes WUSCHEL (WUS) and CLAVATA3 (CLV3) depend on PSS1. PSS1 plays essential roles in inflorescence meristem maintenance through the WUS-CLV pathway, and in leaf and internode development by differentially regulating the class I KNOX genes. PSS1 is involved in a lot of developmental processes and is vital for postembryonic development of Arabidopsis thaliana. PSS1 regulates auxin distribution during leaf development
physiological function
the primary role of PSS enzymes is (3-sn-phosphatidyl)-L-serine biosynthesis, and isozyme PPS1 regulates post-Golgi vesicle secretion to intercellular spaces, the enzyme function is associated with exocytosis. Isozyme PSS1 plays a potential role in mediating cell expansion by regulating secretion of cell wall components