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Literature summary extracted from

  • Samadi, N.; Bekele, R.; Capatos, D.; Venkatraman, G.; Sariahmetoglu, M.; Brindley, D.N.
    Regulation of lysophosphatidate signaling by autotaxin and lipid phosphate phosphatases with respect to tumor progression, angiogenesis, metastasis and chemo-resistance (2011), Biochimie, 93, 61-70.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.106 membrane the active site of the enzyme is on the outer surface of plasma membranes, or the lumenal surface of internal membranes Mus musculus 16020
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Organism

EC Number Organism UniProt Comment Textmining
3.1.3.106 Mus musculus
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-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.106 lysophosphatidate + H2O
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 Mus musculus monoacylglycerol + phosphate
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 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.106 lipid phosphate phosphatase
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 Mus musculus
3.1.3.106 LPP
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 Mus musculus

Expression

EC Number Organism Comment Expression
3.1.3.106 Mus musculus the expression of lipid phosphate phosphatases is decreased in many tumors down

General Information

EC Number General Information Comment Organism
3.1.3.106 physiological function the low expression of lipid phosphate phosphatase in many tumor cells makes them hypersensitive to growth promoting and survival signals that are provided by lysophosphatidate, S1P, platelet-derived growth factor and epidermal growth factor. The intracellular actions of the enzyme controls cell migration, division, angiogenesis and chemoresistance. Increased LPP1 expression attenuates lysophosphatidate-induced migration of fibroblasts Mus musculus