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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: Q6T4P5
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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
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lipid phosphate phosphatase-related protein type 3
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plasticity related gene 3
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acid phosphatidyl phosphatase
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-
-
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ecto-PAPase
-
-
-
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ecto-phosphatidic acid phosphohydrolase
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-
-
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Germ cell guidance factor
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-
-
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PA phosphatase
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-
-
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PAP
-
-
-
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phosphatidate phosphohydrolase
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-
-
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phosphatidic acid phosphatase
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-
-
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phosphatidic acid phosphohydrolase
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-
-
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Wunen protein
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
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
-
-
-
?
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
?
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LPR-3; LPR-3
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isozyme LPP-1, containing the apical sorting signal FDKTRL, is mainly located at the apical surface membrane, while isozyme LPP-3 is located at the basolateral membrane being targeted by the dityrosine motif in the second cytoplasmic portion
Manually annotated by BRENDA team
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLPR3_HUMAN
718
0
76037
Swiss-Prot
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
N-glycosylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of LPP-3 in HEK293 cells and in Xenopus laevis dorsal blastomeres of embryos causing a mild ventralizing effect
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