BRENDA - Enzyme Database

Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns

Donkor, J.; Sariahmetoglu, M.; Dewald, J.; Brindley, D.N.; Reue, K.; J. Biol. Chem. 282, 3450-3457 (2007)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
3.1.3.4
expression of lipin-1, lipin-2, and lipin-3 in HEK-293 cells
Mus musculus
Engineering
EC Number
Amino acid exchange
Commentary
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
Commentary
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
Commentary
Organism
Structure
3.1.3.4
Mg2+
all lipins are dependent on Mg2+
Mus musculus
3.1.3.4
Mg2+
dependent on
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
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
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.4
additional information
lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis
680849
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
680849
Saccharomyces cerevisiae
?
-
-
-
-
3.1.3.4
phosphatidic acid + H2O
-
680849
Mus musculus
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
-
680849
Saccharomyces cerevisiae
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
lipin-1, lipin-2, and lipin-3
680849
Mus musculus
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
Subunits
EC Number
Subunits
Commentary
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
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
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
Commentary
Organism
3.1.3.4
6.5
-
assay at
Mus musculus
3.1.3.4
6.5
-
assay at
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.3.4
expression of lipin-1, lipin-2, and lipin-3 in HEK-293 cells
Mus musculus
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
3.1.3.4
additional information
livers of lipin-1-deficient mice exhibit normal PAP1 activity
Mus musculus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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 (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
Mg2+
all lipins are dependent on Mg2+
Mus musculus
3.1.3.4
Mg2+
dependent on
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
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) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.4
additional information
lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis
680849
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
680849
Saccharomyces cerevisiae
?
-
-
-
-
3.1.3.4
phosphatidic acid + H2O
-
680849
Mus musculus
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
-
680849
Saccharomyces cerevisiae
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
lipin-1, lipin-2, and lipin-3
680849
Mus musculus
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
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
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.1.3.4
37
-
assay at
Mus musculus
3.1.3.4
37
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.3.4
6.5
-
assay at
Mus musculus
3.1.3.4
6.5
-
assay at
Saccharomyces cerevisiae