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Literature summary extracted from

  • Donkor, J.; Sariahmetoglu, M.; Dewald, J.; Brindley, D.N.; Reue, K.
    Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns (2007), J. Biol. Chem., 282, 3450-3457.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.4 expression of lipin-1, lipin-2, and lipin-3 in HEK-293 cells Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.4 additional information livers of lipin-1-deficient mice exhibit normal PAP1 activity Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.4 additional information
-
additional information kinetics of the PAP1 activities of the three lipin proteins, surface dilution kinetic model using micelles of Triton X-100, each lipin exhibits a strong positive cooperativity for phosphatidic acid Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.4 Mg2+ dependent on Saccharomyces cerevisiae
3.1.3.4 Mg2+ all lipins are dependent on Mg2+ Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.4 additional information Mus musculus lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis ?
-
?
3.1.3.4 additional information Saccharomyces cerevisiae lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis ?
-
?
3.1.3.4 phosphatidic acid + H2O Mus musculus
-
1,2-diacyl-sn-glycerol + phosphate
-
?
3.1.3.4 phosphatidic acid + H2O Saccharomyces cerevisiae
-
1,2-diacyl-sn-glycerol + phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.4 Mus musculus
-
three lipins, C57BL/6J and BALB/cByJ-Lpin1+/fld mice
-
3.1.3.4 Saccharomyces cerevisiae
-
a single lipin homolog, Smp2
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.4 brown adipose tissue
-
Mus musculus
-
3.1.3.4 liver
-
Mus musculus
-
3.1.3.4 additional information tissue expression patterns of lipin isozymes, overview, lipin-1 is responsible for PAP1 activity in adipose tissue and skeletal muscle Mus musculus
-
3.1.3.4 skeletal muscle
-
Mus musculus
-
3.1.3.4 white adipose tissue
-
Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.4 additional information lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis Mus musculus ?
-
?
3.1.3.4 additional information lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis Saccharomyces cerevisiae ?
-
?
3.1.3.4 phosphatidic acid + H2O
-
Mus musculus 1,2-diacyl-sn-glycerol + phosphate
-
?
3.1.3.4 phosphatidic acid + H2O
-
Saccharomyces cerevisiae 1,2-diacyl-sn-glycerol + phosphate
-
?
3.1.3.4 phosphatidic acid + H2O lipin-1, lipin-2, and lipin-3 Mus musculus 1,2-diacyl-sn-glycerol + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.3.4 More yeast PAH1 protein sequence contains a haloacid dehalogenase domain, which includes a DXDXT motif found in a superfamily of Mg2+-dependent phosphatases Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
3.1.3.4 lipin-1
-
Mus musculus
3.1.3.4 lipin-1
-
Saccharomyces cerevisiae
3.1.3.4 lipin-2
-
Mus musculus
3.1.3.4 lipin-3
-
Mus musculus
3.1.3.4 PAP1
-
Mus musculus
3.1.3.4 PAP1
-
Saccharomyces cerevisiae
3.1.3.4 phosphatidate phosphatase type-1
-
Mus musculus
3.1.3.4 phosphatidate phosphatase type-1
-
Saccharomyces cerevisiae
3.1.3.4 SMP2
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.4 37
-
assay at Mus musculus
3.1.3.4 37
-
assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.4 6.5
-
assay at Mus musculus
3.1.3.4 6.5
-
assay at Saccharomyces cerevisiae