Information on EC 2.7.8.29 - L-serine-phosphatidylethanolamine phosphatidyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.8.29
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RECOMMENDED NAME
GeneOntology No.
L-serine-phosphatidylethanolamine phosphatidyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-1-phosphatidylethanolamine + L-serine = L-1-phosphatidylserine + ethanolamine
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phosphatidylethanolamine biosynthesis III
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phosphatidylserine biosynthesis II
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superpathway of phospholipid biosynthesis II (plants)
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Glycerophospholipid metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
L-1-phosphatidylethanolamine:L-serine phosphatidyltransferase
This mammalian enzyme catalyses an exchange reaction in which the polar head group of phosphatidylethanolamine is replaced by L-serine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-diacylphosphatidylethanolamine + L-serine
?
show the reaction diagram
the substrate is 6times better utilized than phosphatidylethanolamine plasmalogen
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?
L-1-phosphatidylcholine + L-serine
L-1-phosphatidylserine + choline
show the reaction diagram
L-1-phosphatidylethanolamine + L-serine
L-1-phosphatidylserine + ethanolamine
show the reaction diagram
phosphatidylethanolamine plasmalogen + L-serine
?
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-1-phosphatidylcholine + L-serine
L-1-phosphatidylserine + choline
show the reaction diagram
L-1-phosphatidylethanolamine + L-serine
L-1-phosphatidylserine + ethanolamine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3-sn-phosphatidyl)-L-serine
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end-product inhibition of isozyme PSS1; strong end-product inhibition of isozyme PSS1
phosphatidylserine
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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phosphatidylserine biosynthesis in Chinese hamster ovary cells increases 2.5fold during UV-induced apoptosis. When cells are exposed to UV light to induce apoptosis, phosphatidylserine biosynthesis is stimulated 2fold in PSS II-expressing cells
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
L-serine
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pH 7.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.26
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substrate L-serine, pH 7.5, 37°C
0.51
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substrate L-1-phosphatidylethanolamine, pH 7.5, 37°C
1
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pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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high level of expression
Manually annotated by BRENDA team
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high level of expression
Manually annotated by BRENDA team
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high level of expression
Manually annotated by BRENDA team
additional information
isozyme PSS1 is ubiquitously expressed; isozyme PSS2 is expressed in a tissue-specific manner. It is highly expressed in tissues such as brain and testis, where docosahexaenoic acid (DHA, 22:6n-3) is also highly enriched
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
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x * 55000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anti-FLAG M2 affinity gel chromatography; purification of functional recombinant FLAG-tagged PSS2 from HEK-293 and CHO-K1 cell microsomes by ultracentrifugation, immunoaffinity chromatography
epitope-tagged recombinant protein
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recombinant protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293 cells; gene PTDSS2, functional recombinant overexpression of FLAG-tagged PSS2 isozyme in HEK-293 and CHO-K1 cells
expression in CHO cell and Sf9 cell
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expression in HeLa cell
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expression in McArdle cell and in ethanolamine-requiring mutant Chinese hamster ovary cells defective in PSS1, EC 2.7.8.29
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expression of FLAG- and HA peptide-tagged form
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gene PTDSS1
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gene PTDSS1; gene PTDSS1, expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
docosahexaenoic acid positively modulates phosphatidylserine biosynthesis but does not affect mRNA levels of PSS2
the mRNA expression of phosphatidylserine synthase 1, EC 2.7.8.8, and PSS2 is not reduced by ethanol
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R97K
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in contrast to the PSS II wild-type transformant, the R97K transformant exhibits 4fold higher phosphatidylserine biosynthetic activity than that in CHO-K1 cells. The phosphatidylserine biosynthesis in the R97K transformant is not inhibited at all but elevated by the addition of phosphatidylserine
L265P
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naturally gain-of-function mutation mutation of PSS1
P269L
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naturally gain-of-function mutation mutation of PSS1
P269S
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naturally gain-of-function mutation mutation of PSS1
Q353R
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naturally gain-of-function mutation mutation of PSS1, which resides in a separate cytosolic domain and has only s slight effect on enzyme activity
W277R
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naturally occuring mutation in gene PTDSS1 causing Lenz-Majewski hyperostotic dwarfism with hyperphosphoserinuria, the patient shows hyperostosis and osteosclerosis resulting from accelerated bone formation, and increased PTDS biosynthesis caused by the PTDSS1 mutation leading to hyperphosphoserinuria, phenotype
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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the phosphatidylserine biosynthetic activity of brain, especially for 18:0, 22:6-phosphatidylserine production, is hampered significantly by maternal exposure to ethanol. Phosphatidylserine levels are consistently reduced significantly in brain cortices of the pups from ethanol-exposed dams, due mainly to the depletion of 18:0, 22:6-phosphatidylserine. The mRNA expression of phosphatidylserine synthase 1, EC 2.7.8.8, and PSS2 is not reduced by ethanol