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Literature summary extracted from

  • Zhang, Q.X.; Pilquil, C.S.; Dewald, J.; Berthiaume, L.G.; Brindley, D.N.
    Identification of structurally important domains of lipid phosphate phosphatase-1: implications for its sites of action (2000), Biochem. J., 345, 181-184.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.4 expression of wild-type and mutant enzymes in rat2 fibroblasts Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.4 G170A 38% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 H171L 2% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 H223L 2% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 I233T 94% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 K120R 5% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 L106S 85% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 N142Q 89% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate, mutation decreases the molecular weight by about 4000 Da Mus musculus
3.1.3.4 N276Q 112% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 P128I 2% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 R127K 2% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 R217K 2% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 S169T 0.4% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 T116I 91% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 T122S 97% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 T5P 85% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 Y168F 87% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus
3.1.3.4 Y221W 51% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.4 plasma membrane active site located on the outer surface Mus musculus 5886
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.4 Mus musculus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.3.4 glycoprotein glycosylation is not required for activity Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.4 lysophosphatidic acid + H2O
-
 Mus musculus monoacylglycerol + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.4 lipid phosphate phosphatase-1
-
 Mus musculus
3.1.3.4 LPP-1
-
 Mus musculus