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Information on EC 2.7.8.29 - L-serine-phosphatidylethanolamine phosphatidyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9BVG9
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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: Homo sapiens
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
-
-, -, -, -
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
L-1-phosphatidylcholine + L-serine
L-1-phosphatidylserine + choline
isozyme PSS1
-
-
r
L-1-phosphatidylethanolamine + L-serine
L-1-phosphatidylserine + ethanolamine
-
-
-
?
L-1-phosphatidylethanolamine + L-serine
L-1-phosphatidylserine + ethanolamine
isozyme PSS2
-
-
r
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
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3-sn-phosphatidyl)-L-serine
end-product inhibition of isozyme PSS1
(3-sn-phosphatidyl)-L-serine
strong end-product inhibition of isozyme PSS1
additional information
addition of phosphatidylcholine instead of phosphatidylserine does not reduce the rate of phosphatidylserine synthesis
-
additional information
addition of phosphatidylcholine instead of phosphatidylserine does not reduce the rate of phosphatidylserine synthesis
-
additional information
-
addition of phosphatidylcholine instead of phosphatidylserine does not reduce the rate of phosphatidylserine synthesis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
integral membrane protein, membrane topology overview
integral membrane protein, membrane topology overview
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
link between phosphatidylserine synthesis and bone metabolism
malfunction
metabolism
link between phosphatidylserine synthesis and bone metabolism
physiological function
malfunction
gain-of-function mutation of PTDSS1 encoding phosphatidylserine synthase 1, a causative heterozygous missense mutations in gene PTDSS1, causes Lenz-Majewski syndrome (LMS), a syndrome of intellectual disability and multiple congenital anomalies that features generalized craniotubular hyperostosis. End-product inhibition of PSS1 by phosphatidylserine is markedly reduced in the mutant. The gain-of-function mutation is associated with regulatory dysfunction of PSS1. Phenotypes, overview
malfunction
mutation W277R of PTDSS1 encoding phosphatidylserine synthase 1 causes Lenz-Majewski hyperostotic dwarfism with hyperphosphoserinuria. Lenz-Majewski hyperostotic dwarfism (LMHD) is an ultra-rare Mendelian craniotubular dysostosis that causes skeletal dysmorphism and widely distributed osteosclerosis. In vivo, PTDSS1 defects cause LMHD and support enhanced biosynthesis of PTDS in the pathogenesis of LMHD, while in vitro, these PTDSS1 mutations are gain-of-function and increase PTDS production. Phenotype, overview
physiological function
-
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
isozyme PSS1 is one of two enzymes involved in the production of phosphatidylserine
physiological function
isozyme PSS1 promotes the biosynthesis of phosphatidylserine (PTDS), which is a functional constituent of lipid bilayers. PTDS binds calcium within matrix vesicles to engender hydroxyapatite crystal formation, and may enhance mesenchymal stem cell differentiation leading to osteogenesis
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_HUMAN
487
7
56253
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q353R
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
docosahexaenoic acid positively modulates phosphatidylserine biosynthesis but does not affect mRNA levels of PSS2
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Tomohiro, S.; Kawaguti, A.; Kawabe, Y.; Kitada, S.; Kuge, O.
Purification and characterization of human phosphatidylserine synthases 1 and 2
Biochem. J.
418
421-429
2009
Homo sapiens (Q9BVG9)
Whyte, M.P.; Blythe, A.; McAlister, W.H.; Nenninger, A.R.; Bijanki, V.N.; Mumm, S.
Lenz-Majewski hyperostotic dwarfism with hyperphosphoserinuria from a novel mutation in PTDSS1 encoding phosphatidylserine synthase 1
J. Bone Miner. Res.
30
606-614
2015
Homo sapiens (P48651), Homo sapiens
Sousa, S.B.; Jenkins, D.; Chanudet, E.; Tasseva, G.; Ishida, M.; Anderson, G.; Docker, J.; Ryten, M.; Sa, J.; Saraiva, J.M.; Barnicoat, A.; Scott, R.; Calder, A.; Wattanasirichaigoon, D.; Chrzanowska, K.; Simandlova, M.; Van Maldergem, L.; Stanier, P.; Beales, P.L.; Vance, J.E.; Moore, G.E.
Gain-of-function mutations in the phosphatidylserine synthase 1 (PTDSS1) gene cause Lenz-Majewski syndrome
Nat. Genet.
46
70-76
2014
Homo sapiens (P48651), Homo sapiens (Q9BVG9), Homo sapiens
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