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Information on EC 2.7.8.29 - L-serine-phosphatidylethanolamine phosphatidyltransferase and Organism(s) Mus musculus and UniProt Accession Q9Z1X2
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2.7.8.29 L-serine-phosphatidylethanolamine phosphatidyltransferaseIUBMB Comments
This mammalian enzyme catalyses an exchange reaction in which the polar head group of phosphatidylethanolamine is replaced by L-serine.
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Word Map
- 2.7.8.29
- phospholipid
- lm
-
intellectual
-
docosahexaenoic
-
osteosclerosis
-
craniofacial
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
ptdss1, pss-2, ptdss2, ps synthase 1, phosphatidylserine synthase 2, pssii, ps synthase 2, ptdser synthase 2, phosphatidylserine synthetase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
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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.
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
1,2-diacylphosphatidylethanolamine + L-serine
?
the substrate is 6times better utilized than phosphatidylethanolamine plasmalogen
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-
?
L-1-phosphatidylcholine + L-serine
L-1-phosphatidylserine + choline
isozyme PSS1
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-
r
L-1-phosphatidylethanolamine + L-serine
L-1-phosphatidylserine + ethanolamine
-
-
-
?
L-1-phosphatidylethanolamine + L-serine
L-1-phosphatidylserine + ethanolamine
-
-
-
?
L-1-phosphatidylethanolamine + L-serine
L-1-phosphatidylserine + ethanolamine
isozyme PSS2
-
-
r
additional information
?
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the recombinant FLAG-tagged enzyme is also active with phosphatidylethanolamine plasmalogen, [C18(plasm),22:6-PS], which is six times less effective as a substrate than the corresponding ester-linked phosphatidylethanolamine species, the isozyme is active with oleic acid (OA; 18:1n-9), DHA (DHA; 22:6n-3), or arachidonic acid esters. Compounds analysis by mass spectroscopy. A carbonyl group next to the glycerol backbone in the substrate-binding pocket substantially increases the catalytic activity of PSS2. Isozyme PSS2 shows a 10fold preference for sn-1 18:0, when 22:6 is esterified at the sn-2 position. Synthesis of 18:0,22:6-PS is most efficient compared with 18:0,18:1-PS and with 18:0,20:4-PS. Substrate specificity and acyl chain preference of isozyme PS2, overview
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?
additional information
?
-
the recombinant FLAG-tagged enzyme is also active with phosphatidylethanolamine plasmalogen, [C18(plasm),22:6-PS], which is six times less effective as a substrate than the corresponding ester-linked phosphatidylethanolamine species, the isozyme is active with oleic acid (OA; 18:1n-9), DHA (DHA; 22:6n-3), or arachidonic acid esters. Compounds analysis by mass spectroscopy. A carbonyl group next to the glycerol backbone in the substrate-binding pocket substantially increases the catalytic activity of PSS2. Isozyme PSS2 shows a 10fold preference for sn-1 18:0, when 22:6 is esterified at the sn-2 position. Synthesis of 18:0,22:6-PS is most efficient compared with 18:0,18:1-PS and with 18:0,20:4-PS. Substrate specificity and acyl chain preference of isozyme PS2, overview
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?
additional information
?
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the recombinant FLAG-tagged enzyme is also active with phosphatidylethanolamine plasmalogen, [C18(plasm),22:6-PS], which is six times less effective as a substrate than the corresponding ester-linked phosphatidylethanolamine species, the isozyme is active with oleic acid (OA; 18:1n-9), DHA (DHA; 22:6n-3), or arachidonic acid esters. Compounds analysis by mass spectroscopy. A carbonyl group next to the glycerol backbone in the substrate-binding pocket substantially increases the catalytic activity of PSS2. Isozyme PSS2 shows a 10fold preference for sn-1 18:0, when 22:6 is esterified at the sn-2 position. Synthesis of 18:0,22:6-PS is most efficient compared with 18:0,18:1-PS and with 18:0,20:4-PS. Substrate specificity and acyl chain preference of isozyme PS2, overview
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?
additional information
?
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-
the enzyme synthesizes docosahexaenoic acid-phosphatidylserine much more efficiently than phosphatidylserine containing either 18:1 or 20:4 at the sn-2 position. Although no sn-1 fatty acyl preference is noted, phosphatidylserine synthase 2 exhibits significant preference toward docosahexaenoic acid compared with 18:1 or 20:4 at the sn-2 position
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-
?
additional information
?
-
the enzyme synthesizes docosahexaenoic acid-phosphatidylserine much more efficiently than phosphatidylserine containing either 18:1 or 20:4 at the sn-2 position. Although no sn-1 fatty acyl preference is noted, phosphatidylserine synthase 2 exhibits significant preference toward docosahexaenoic acid compared with 18:1 or 20:4 at the sn-2 position
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-
?
additional information
?
-
the enzyme synthesizes docosahexaenoic acid-phosphatidylserine much more efficiently than phosphatidylserine containing either 18:1 or 20:4 at the sn-2 position. Although no sn-1 fatty acyl preference is noted, phosphatidylserine synthase 2 exhibits significant preference toward docosahexaenoic acid compared with 18:1 or 20:4 at the sn-2 position
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-
?
additional information
?
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-
isozyme PSS1 shows a 2fold higher preference for sn-1 18:0 compared with 16:0 when the sn-2 position contains 18:1
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-
?
additional information
?
-
isozyme PSS1 shows a 2fold higher preference for sn-1 18:0 compared with 16:0 when the sn-2 position contains 18:1
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-
?
additional information
?
-
isozyme PSS1 shows a 2fold higher preference for sn-1 18:0 compared with 16:0 when the sn-2 position contains 18:1
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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
L-1-phosphatidylethanolamine + L-serine
L-1-phosphatidylserine + ethanolamine
isozyme PSS2
-
-
r
L-1-phosphatidylcholine + L-serine
L-1-phosphatidylserine + choline
isozyme PSS1
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-
r
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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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
additional information
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
additional information
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
phosphatidylserine is synthesized in mammalian cells by two integral membrane proteins, PS synthase 1 and 2 (PSS1 and PSS2). These enzymes catalyze the formation of phosphatidylserine by an exchange reaction in which serine replaces the head group of the corresponding substrate phospholipids, phosphatidylcholine (PC) for isozyme PSS1 and phosphatidylethanolamine (PE) for isozyme PSS2
physiological function
metabolism
phosphatidylserine is synthesized in mammalian cells by two integral membrane proteins, PS synthase 1 and 2 (PSS1 and PSS2). These enzymes catalyze the formation of phosphatidylserine by an exchange reaction in which serine replaces the head group of the corresponding substrate phospholipids, phosphatidylcholine (PC) for isozyme PSS1 and phosphatidylethanolamine (PE) for isozyme PSS2
physiological function
physiological function
expression of PSS2 in ethanolamine-requiring mutant Chinese hamster ovary cells defective in PSS1, reverses the ethanolamine auxotrophy. However, the phosphatidylethanolamine content is not normalized unless the culture medium is supplemented with ethanolamine. In both mutant chinese hamster ovary cells and hepatoma cells transfected with PSS2 cDNA the rate of synthesis of phosphatidylserine and phosphatidylserine-derived phosphatidylethanolamine does not exceed that in parental chinese hamster ovary cells or control McArdle cells, respectively. Expression of murine PSS2 in McArdle cells does not inhibit phosphatidylethanolamine synthesis via the CDP-ethanolamine pathway, whereas expression of similar levels of PSS1 activity inhibit this pathway by approx. 50%
physiological function
isozyme PSS2 may play a key role in phosphatidylserine accumulation in brain and testis through high activity toward DHA-containing substrates that are abundant in these tissues
physiological function
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docosahexaenoic acid positively modulates phosphatidylserine biosynthesis. Over-expression of PSS2 alters neither the phosphatidylserine level nor the effect of docosahexaenoic acid on phosphatidylserine increase
physiological function
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intercrosses of mice lacking PSS1, EC 2.7.8.8, and PSS2-/- mice yield mice with three disrupted Pss alleles but no double knockout mice. In PSS1-/-PSS2+/- and PSS1+/-PSS2-/- mice, serine exchange activity is reduced by 65-91%,and the tissue content of phosphatidylserine and phosphatidylethanolamine is also decreased. Elimination of either PSS1 or PSS2, but not both, is compatible with mouse viability, mice can tolerate as little as 10% of normal total serine-exchange activity, and mice survive with significantly reduced phosphatidylserine and phosphatidylethanolamine content
physiological function
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the ability of testis extracts from PSS2-deficient mice to catalyze serine exchange is reduced by more than 95%, reductions of 90% are found in the brain and liver. There are no perturbations in the phospholipid content of any of these tissues. The expression of PSS1, EC 2.7.8.8, is not upregulated in Pss2-deficient cells and tissues. Testis weight is reduced in Pss2-deficient mice, and some of the male mice are infertile
physiological function
the enzyme plays a key role in phosphatidylserine accumulation in brain and testis through high activity toward docosahexaenoic acid-containing substrates
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PTSS2_MOUSE
473
7
55021
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of functional recombinant FLAG-tagged PSS2 from HEK-293 and CHO-K1 cell microsomes by ultracentrifugation, immunoaffinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in McArdle cell and in ethanolamine-requiring mutant Chinese hamster ovary cells defective in PSS1, EC 2.7.8.29
gene PTDSS2, functional recombinant overexpression of FLAG-tagged PSS2 isozyme in HEK-293 and CHO-K1 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
docosahexaenoic acid positively modulates phosphatidylserine biosynthesis but does not affect mRNA levels of PSS2
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arikketh, D.; Nelson, R.; Vance, J.E.
Defining the importance of phosphatidylserine synthase-1 (PSS1): unexpected viability of PSS1-deficient mice
J. Biol. Chem.
283
12888-12897
2008
Mus musculus
Guo, M.; Stockert, L.; Akbar, M.; Kim, H.Y.
Neuronal specific increase of phosphatidylserine by docosahexaenoic acid
J. Mol. Neurosci.
33
67-73
2007
Cricetulus griseus (O08888), Homo sapiens, Mus musculus
Stone, S.J.; Vance, J.E.
Cloning and expression of murine liver phosphatidylserine synthase (PSS)-2: differential regulation of phospholipid metabolism by PSS1 and PSS2
Biochem. J.
342
57-64
1999
Mus musculus (Q9Z1X2)
Bergo, M.O.; Gavino, B.J.; Steenbergen, R.; Sturbois, B.; Parlow, A.F.; Sanan, D.A.; Skarnes, W.C.; Vance, J.E.; Young, S.G.
Defining the importance of phosphatidylserine synthase 2 in mice
J. Biol. Chem.
277
47701-47708
2002
Mus musculus
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