WordNet

any of a group of enzymes that act as a catalyst in the hydrolysis of organic phosphates

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/03/30 00:56:35」(JST)

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In enzymology, a phosphatidate phosphatase (EC 3.1.3.4) is an enzyme that catalyzes the chemical reaction:^[1]

a 3-sn-phosphatidate + H₂O a 1,2-diacyl-sn-glycerol + phosphate

Thus, the two substrates of this enzyme are 3-sn-phosphatidate and H₂O, whereas its two products are 1,2-diacyl-sn-glycerol and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. This enzyme participates in 4 metabolic pathways: glycerolipid, glycerophospholipid, ether lipid, and sphingolipid metabolism.

Nomenclature

The systematic name of this enzyme class is 3-sn-phosphatidate phosphohydrolase. Other names in common use include:

phosphatidic acid phosphatase (PAP),
acid phosphatidyl phosphatase,
phosphatidic acid phosphohydrolase,
phosphatidate phosphohydrolase, and
lipid phosphate phosphohydrolase (LPP).

Types

There are several different genes that codify for phosphatidate phosphatases. They been classified in two groups (type I and type II) based on their cellular localization and substrate specificity.^[2]

Type I

Type I phosphatidate phosphatases are soluble enzymes that can associate to membranes. There are found mainly in the cytosol and the nucleus. Codified by a group of genes named Lipin they are substrate specific only to phosphatidate. There are speculated to be involved in the de novo synthesis of glycerolipids.

Type II

Type II phosphatidate phospatases are transmembrane enzymes found mainly in the plasma membrane. They can also dephosphorylate other substrates beside phosphatidate therefore are also known as lipid-phosphate phosphatase. Their main role is in lipid signaling and in phospholipid head-group remodeling.

Genes

Human genes that encode phosphatidate phosphatases include:

PPAP2A (LPP1) – phosphatidic acid phosphatase type 2A
PPAP2B (LPP3) – phosphatidic acid phosphatase type 2B
PPAP2C (LPP2) – phosphatidic acid phosphatase type 2C
PPAPDC1A (PPC1A) – phosphatidic acid phosphatase type 2 domain containing 1A
PPAPDC1B (PPC1B) – phosphatidic acid phosphatase type 2 domain containing 1B
PPAPDC2 – phosphatidic acid phosphatase type 2 domain containing 2
PPAPDC3 – phosphatidic acid phosphatase type 2 domain containing 3
LPPR2 – lipid phosphate phosphatase-related protein type 2
LPPR3 – lipid phosphate phosphatase-related protein type 3
LPPR4 – lipid phosphate phosphatase-related protein type 4
LPIN1 – lipin 1^[3]^[4]
LPIN2 – lipin 2^[4]
LPIN3 – lipin 3^[4]

References

^ Smith SW, Weiss SB, Kennedy EP (October 1957). "The enzymatic dephosphorylation of phosphatidic acids". J. Biol. Chem. 228 (2): 915–22. PMID 13475370.
^ Carman GM, Han GS (December 2006). "Roles of phosphatidate phosphatase enzymes in lipid metabolism". Trends Biochem. Sci. 31 (12): 694–9. doi:10.1016/j.tibs.2006.10.003. PMC 1769311. PMID 17079146.
^ Han GS, Wu WI, Carman GM (April 2006). "The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme". J. Biol. Chem. 281 (14): 9210–8. doi:10.1074/jbc.M600425200. PMC 1424669. PMID 16467296.
^ ^a ^b ^c Donkor J, Sariahmetoglu M, Dewald J, Brindley DN, Reue K (February 2007). "Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns". J. Biol. Chem. 282 (6): 3450–7. doi:10.1074/jbc.M610745200. PMID 17158099.

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3. グルコース-6-ホスファターゼ欠損症（糖原病I型、フォンギールケ病） glucose 6 phosphatase deficiency glycogen storage disease i von gierke disease
4. 幼児期および小児期早期の一過性高リン血症 transient hyperphosphatasemia of infancy and early childhood
5. 慢性腎臓疾患に関連する無形成骨症 adynamic bone disease associated with chronic kidney disease

English Journal

Hypoxia causes triglyceride accumulation via HIF-1-mediated stimulation of lipin 1 expression.

Mylonis I, Sembongi H, Befani C, Liakos P, Siniossoglou S, Simos G.AbstractAdaptation to hypoxia involves the hypoxia-inducible transcription factors HIFs and requires reprogramming of cellular metabolism that is essential during both physiological and pathological processes. In contrast to the established role of HIF-1 in glucose metabolism, the involvement of HIFs and the molecular mechanisms concerning the effects of hypoxia on lipid metabolism are poorly characterized. Here, we report that exposure of human cells to hypoxia causes triglyceride and lipid droplet accumulation. This is accompanied by induction of lipin 1, a phosphatidate phosphatase isoform that catalyzes the penultimate step in triglyceride biosynthesis, while lipin 2 remains unaffected. Hypoxic up-regulation of lipin 1 expression involves predominantly HIF-1, which binds to a single distal hypoxia-responsive element in the lipin 1 gene promoter and causes its activation under low oxygen conditions. Hypoxic triglyceride or lipid droplet accumulation can be blocked by siRNA-mediated silencing of lipin 1 expression or kaempferol-mediated inhibition of HIF-1. We conclude that direct control of lipin 1 transcription by HIF-1 is an important regulatory feature of lipid metabolism and its adaptation to hypoxia.
Journal of cell science.J Cell Sci.2012 Mar 30. [Epub ahead of print]
Adaptation to hypoxia involves the hypoxia-inducible transcription factors HIFs and requires reprogramming of cellular metabolism that is essential during both physiological and pathological processes. In contrast to the established role of HIF-1 in glucose metabolism, the involvement of HIFs and th
PMID 22467849

MicroRNA-217 promotes ethanol-induced fat accumulation in hepatocytes by down-regulating SIRT1.

Yin H, Hu M, Zhang R, Shen Z, Flatow L, You M.SourceDepartment of Molecular Pharmacology, University of South Florida Health Sciences Center, Tampa, Florida 33612, USA.
The Journal of biological chemistry.J Biol Chem.2012 Mar 23;287(13):9817-26. Epub 2012 Feb 3.
Ethanol-mediated inhibition of hepatic sirtuin 1 (SIRT1) plays a crucial role in the pathogenesis of alcoholic fatty liver disease. Here, we investigated the underlying mechanisms of this inhibition by identifying a new hepatic target of ethanol action, microRNA-217 (miR-217). The role of miR-217 in
PMID 22308024

Japanese Journal

脂質代謝におけるＬｉｐｉｎ１

YAKUGAKU ZASSHI 131(8), 1189-1194, 2011
NAID 130001075907

The Saccharomyces cerevisiae Lipin homolog is a Mg[2+]-dependent phosphatidate phosphatase enzyme

J. Biol. Chem. 281, 9210-9218, 2006
NAID 80019231496

Isolation and characterization of the Saccharomyces cerevisiae LPP1 gene encoding a Mg^<2+>-independent phosphatidate phosphatase.

J. Biol. Chem. 273, 14331-14338, 1998
NAID 30016306409

「ホスファチジン酸ホスファターゼ」

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phosphatidate phosphatase
Identifiers
EC number	3.1.3.4
CAS number	9025-77-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
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PMC	articles
PubMed	articles
NCBI	proteins