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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: Q14693
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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
phosphatidate phosphatase
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
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
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
lipin-1 is negatively regulated by phosphorylation during mitosis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
may partly substitute for Mg2+ in binding to to serine/threonine protein phosphatase-1 catalytic subunit
Mg2+
lipin-1 binding to to serine/threonine protein phosphatase-1 catalytic subunit depends on presence of Mg2+
Mn2+
may substitute for Mg2+ in binding to to serine/threonine protein phosphatase-1 catalytic subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
mitotic phosphorylation of lipin 1 inhibits its phosphatidic acid phosphatase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PAP1 activity increases during adipogenesis
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
isoform lipin-1 binds to serine/threonine protein phosphatase-1 catalytic subunit through a HVRF binding motif. Mutating the HVRF motif in the highly conserved N terminus of lipin-1 greatly decreases serine/threonine protein phosphatase-1 catalytic subunit interaction. Mutations of other residues in the N terminus of lipin-1 also modulate serine/threonine protein phosphatase-1 catalytic subunit binding. Serine/threonine protein phosphatase-1 catalytic subuni binds poorly to a phosphomimetic mutant of lipin-1 andbinds well to the non-phosphorylatable lipin-1 mutant. Mutating the HVRFmotif also abrogates the nuclear translocation and phosphatidate phosphatase activity of lipin-1
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LPIN1_HUMAN
890
0
98664
Swiss-Prot
other Location (Reliability: 3)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
mitotic phosphorylation of lipin 1 inhibits its phosphatidic acid phosphatase activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D712E/D714E
catalytically inactive. Mutant binds to serine/threonine protein phosphatase-1 catalytic subunit to the same extent as wild-type
F87A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to n intermediate phenotype in binding to serine/threonine protein phosphatase-1 catalytic subunit
I67A/I69A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to a decrase in binding to serine/threonine protein phosphatase-1 catalytic subunit
L58A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit
L80A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to n intermediate phenotype in binding to serine/threonine protein phosphatase-1 catalytic subunit
V57A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit
V64A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit
additional information
mutation of the HVRF binding motif to HARA causes a decrease in binding to serine/threonine protein phosphatase-1 catalytic subunit, blocks nuclear localization and phosphatidate phosphatase activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HEK-293 cell
expression of lipin-1 in HeLa M cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grimsey, N.; Han, G.S.; OHara, L.; Rochford, J.J.; Carman, G.M.; Siniossoglou, S.
Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2
J. Biol. Chem.
283
29166-29174
2008
Mus musculus, Homo sapiens (Q14693)
Manually annotated by BRENDA team
Kok, B.P.; Skene-Arnold, T.D.; Ling, J.; Benesch, M.G.; Dewald, J.; Harris, T.E.; Holmes, C.F.; Brindley, D.N.
Conserved residues in the N terminus of lipin-1 are required for binding to protein phosphatase-1c, nuclear translocation, and phosphatidate phosphatase activity
J. Biol. Chem.
289
10876-10886
2014
Homo sapiens (Q14693)
Manually annotated by BRENDA team