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Information on EC 2.7.8.8 - CDP-diacylglycerol-serine O-phosphatidyltransferase
for references in articles please use BRENDA:EC2.7.8.8
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.8 Transferases for other substituted phosphate groups
2.7.8.8 CDP-diacylglycerol-serine O-phosphatidyltransferase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 2.7.8.8
- phospholipid
- phosphatidylethanolamine
- phosphatidylcholine
- cardiolipin
- phosphatidylglycerol
- cytidylyltransferase
- phosphatidylglycerophosphate
- cdp-ethanolamine
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ptdetn
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3-phosphatidyltransferase
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uasino
- ptdss1
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phospholipid-synthesizing
- food industry
showSynonyms
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
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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
MetaCyc
phosphatidylserine and phosphatidylethanolamine biosynthesis I, superpathway of phospholipid biosynthesis II (plants)
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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
LITERATURE
COMMENTARY
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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Substrates: 41% of the activity compared to CDP-1,2-diacylglycerol with fatty acids from lecithin
Products: -
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?
CDP-1,2-diacylglycerol + L-serine
CMP + 1,2-diacyl-sn-glycerol-3-phospho-L-serine
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Substrates: fatty acids from lecithin
Products: -
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?
CDP-1,2-dicaproyl-DL-glycerol + L-Ser
CMP + 3-O-sn-1,2-dicaproylphosphatidylserine
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Substrates: -
Products: -
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?
CDP-1,2-distearoyl-L-glycerol + L-Ser
CMP + 1,2-distearoylphosphatidylserine
Substrates: -
Products: -
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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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Substrates: 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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Substrates: low activity
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?
CDP-dipalmitoylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
Substrates: -
Products: -
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?
CDP-1,2-dipalmitoyl-L-glycerol + L-Ser
CMP + 1,2-dipalmitoylphosphatidylserine
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Substrates: -
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?
CDP-1,2-dipalmitoyl-L-glycerol + L-Ser
CMP + 1,2-dipalmitoylphosphatidylserine
Substrates: -
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?
CDP-diacylglycerol + H2O
CMP + phosphatidic acid
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Substrates: -
Products: -
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?
CDP-diacylglycerol + H2O
CMP + phosphatidic acid
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Substrates: at 1% of the synthetic rate the enzyme catalyzes the hydrolysis of phosphatidylserine to CMP and phosphatidic acid
Products: -
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CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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Substrates: -
Products: -
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?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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Substrates: -
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?
CDP-diacylglycerol + L-Ser
CMP + 3-O-sn-phosphatidyl-L-serine
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Substrates: 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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Substrates: reaction proceeds with retention of configuration at phosphorus, which suggests a two-step mechanism involving a phosphatidyl-enzyme intermediate
Products: -
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?
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
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Substrates: -
Products: -
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?
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
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Substrates: -
Products: -
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?
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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Substrates: the enzyme participates in the biosynthesis of phosphatidylethanolamine
Products: -
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?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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Substrates: 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
Products: -
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CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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Substrates: 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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Substrates: 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
Products: -
Products: -
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CDP-diacylglycerol + sn-glycero-3-phosphate
CMP + phosphatidylglycerophosphate
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Substrates: -
Products: -
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?
CDP-diacylglycerol + sn-glycero-3-phosphate
CMP + phosphatidylglycerophosphate
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Substrates: low activity
Products: -
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?
additional information
?
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Substrates: the enzyme also catalyzes the exchange reaction between Ser and phosphatidylserine
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?
additional information
?
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Substrates: the enzyme also catalyzes the exchange reaction between Ser and phosphatidylserine
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?
additional information
?
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Substrates: the enzyme also catalyzes the exchange reaction between Ser and phosphatidylserine
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?
additional information
?
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Substrates: enzyme catalyzes exchange reaction between dCDP-diglyceride and dCDP-diglyceride
Products: -
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?
additional information
?
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Substrates: enzyme catalyzes exchange reaction between CMP and CDP-diglyceride
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?
additional information
?
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Substrates: enzyme catalyzes exchange reaction between CMP and CDP-diglyceride
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?
additional information
?
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Substrates: enzyme catalyzes exchange reaction between CMP and CDP-diglyceride
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?
additional information
?
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Substrates: 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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Substrates: 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
Products: -
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + L-serine
CMP + (3-sn-phosphatidyl)-L-serine
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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Substrates: the enzyme participates in the biosynthesis of phosphatidylethanolamine
Products: -
Products: -
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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Substrates: 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
Products: -
Products: -
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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Substrates: the enzyme catalyzes the first committed step in the biosynthesis of phosphatidylethanolamine
Products: -
Products: -
?
CDP-diacylglycerol + L-serine
CMP + 3-O-sn-phosphatidyl-L-serine
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Substrates: 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
Products: -
Products: -
?
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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 40Ā°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 40Ā°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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
physiological function
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expression of Cho1 in a Saccharomyces cerevisiae Cho1 deletion mutant rescues the mutant's growth defect in the absence of ethanolamine supplementation. An Saccharomyces cerevisiae Cho1 deletion mutant expressing Cryptococcus neoformans Cho1 has phosphatidylserine synthase activity. Expression of Cho1 in Cryptococcus neoformans is essential for mitochondrial function and cell viability. Its deficiency cannot be complemented by ethanolamine or choline supplementation
physiological function
-
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
physiological function
knockdown of PSS in Salicornia europaea suspension cells results in reduced phosphatidylserine content, decreased cell survival rate, and increased plasma membrane depolarization and K+ efflux in presence of 400 or 800 mM NaCl. The upregulation of PSS leads to increased phosphatidylserine and phosphatidylethanolamine levels and enhanced salt tolerance in Arabidopsis, along with a lower accumulation of reactive oxygen species, less membrane injury, less plasma membrane depolarization and higher K+/Na+ ratio in the transgenic lines than in wild-type
physiological function
PSS1 regulates post-Golgi vesicle secretion to intercellular spaces. Mutation of PSS1 leads to compromised delivery of CESA4 and sec-GFP towards the cell surface, resulting in weakened intercellular adhesion and disorganized cell arrangement in parenchyma. The phenotype sui1-4 of PSS1 mutants is caused largely by the reduction in cellulose contents in the whole plant and detrimental delivery of pectins in the uppermost internode. PSS1 and product phosphatidylserine localize to organelles associated with exocytosis
physiological function
the phosphatidylserine synthase Cho1-/- and phosphatidylserine decarboxylase Psd1-/- Psd2-/- mutations cause similar changes in levels of phosphatidic acid, phosphatidylglycerol, phosphatidylinositol and phosphatidylserine. Only slight changes are seen in phosphatidylethanolamine and phosphatidylcholine levels. In the Cho1-/- mutant, phosphatidylserine is essentially absent
physiological function
-
transient expression of PSS1 in Nicotiana benthamiana leaves increased phosphatidylserine abundance. Overexpression of PSS1 in an in vivo root transgenic system for sweet potato markedly decreases cellular Na+ accumulation in salinized transgenic roots compared with adventitious roots. The overexpression of PSS1 enhances salt-induced Na+/H+ antiport activity and increases plasma membrane Ca2+-permeable channel sensitivity to NaCl and H2O2 in the transgenic roots. Compared with the wild-type plants, the transgenic lines present decreased Na+ accumulation, enhanced Na+ exclusion, and increased plasma membrane Ca2+-permeable channel sensitivity to NaCl and H2O2 in the roots
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PDB
SCOP
CATH
UNIPROT
ORGANISM