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Information on EC 3.1.3.4 - phosphatidate phosphatase

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.4 phosphatidate phosphatase
IUBMB Comments
This enzyme catalyses the Mg2+-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. In lipid signalling, the enzyme generates a pool of DAG to be used for protein kinase C activation. The mammalian enzymes are known as lipins.
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This record set is specific for:
UNIPROT: Q8TBJ4
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phosphatidate phosphohydrolase, lipin-1, lpin1, pap-1, lipin1, phosphatidate phosphatase, lipin 1, prg-1, phosphatidic acid phosphohydrolase, pa phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipid phosphate phosphatase
-
lipid phosphate phosphatase-related protein type 1
-
lipidphosphatase-related protein 1
-
plasticity related gene 3
-
acid phosphatidyl phosphatase
-
-
-
-
ecto-PAPase
-
-
-
-
ecto-phosphatidic acid phosphohydrolase
-
-
-
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Germ cell guidance factor
-
-
-
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PA phosphatase
-
-
-
-
PAP
-
-
-
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phosphatidate phosphohydrolase
-
-
-
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phosphatidic acid phosphatase
-
-
-
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phosphatidic acid phosphohydrolase
-
-
-
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Wunen protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
diacylglycerol-3-phosphate phosphohydrolase
This enzyme catalyses the Mg2+-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. In lipid signalling, the enzyme generates a pool of DAG to be used for protein kinase C activation. The mammalian enzymes are known as lipins.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-77-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ceramide 1-phosphate + H2O
ceramide + phosphate
show the reaction diagram
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
LPP1 but not LPR1
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
show the reaction diagram
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
RNAi2
reduces expression levels of LPR1 by ca. 60% in SK-OV-3 cells
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
regulation of filopodia by LPR1 is not mediated by cdc42 or Rif, and is independent of the Arp2/3 complex
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LPP-1a predominantly
Manually annotated by BRENDA team
LPP-1 predominantly
Manually annotated by BRENDA team
LPP-1 predominantly
Manually annotated by BRENDA team
LPP-1 predominantly
Manually annotated by BRENDA team
LPP-1 predominantly
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLPR1_HUMAN
325
0
35795
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
LPR1, Western blot analysis
38000
LPR1, Western blot analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
N-glycosylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
LPR1 variants containing non-conservative substitutions of Ser198 and His200 within the C2 motif and Arg246 from the C3 motif are strongly expressed in transient transfection experiments but fail to induce the formation of filopodia in HeLa cells. In contrast to wild-type LPR1, these mutant LPR1 proteins are exclusively localized to intracellular membranes. LPR1 C-term DELTA43 mutant, is incapable of generating new filopodia, but rather localizes to pre-existing endogenous protrusions extended by these cells. Subcellular distribution of mutant LPR1 C-term DELTA43 between the plasma membrane and intracellular membranes is highly comparable with that of wild-type LPR1
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
LPP1 and LPR1 expressed in Sf9 cells using a baculovirus vector. Recombinant LPR1 and mutants incorporating a C-terminal EGFP tag expressed in HeLa and COS7 cells. Overexpression of EGFP-LPR1 in SK-OV-3 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brindley, D.N.
Lipid phosphate phosphatases and related proteins: signaling functions in development, cell division, and cancer
J. Cell. Biochem.
92
900-912
2004
Drosophila melanogaster, Mus musculus, Rattus norvegicus, Homo sapiens (Q6T4P5), Homo sapiens (Q7Z2D5), Homo sapiens (Q8TBJ4), Homo sapiens (Q96GM1)
Manually annotated by BRENDA team
Sigal, Y.J.; Quintero, O.A.; Cheney, R.E.; Morris, A.J.
Cdc42 and ARP2/3-independent regulation of filopodia by an integral membrane lipid-phosphatase-related protein
J. Cell Sci.
120
340-352
2007
Homo sapiens (Q8TBJ4)
Manually annotated by BRENDA team