BRENDA - Enzyme Database

A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase

Karanasios, E.; Han, G.S.; Xu, Z.; Carman, G.M.; Siniossoglou, S.; Proc. Natl. Acad. Sci. USA 107, 17539-17544 (2010)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
3.1.3.4
additional information
dephosphorylation of lipin Pah1p by the Nem1p-Spo7p complex enables the amphipathic helix to anchor Pah1p onto the nuclear/endoplasmic reticulum membrane allowing the production of diacylglycerol for lipid biosynthesis
Saccharomyces cerevisiae
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.1.3.4
0.43
-
phosphatidic acid
wild type enzyme, pH and temperature not specified in the publication
Saccharomyces cerevisiae
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.4
membrane
recruitment of the yeast lipin (Pah1p) is regulated by PA levels onto the nuclear/endoplasmic reticulum membrane. Recruitment requires the transmembrane protein phosphatase complex Nem1p-Spo7p
Saccharomyces cerevisiae
16020
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
Mg2+
dependent on
Saccharomyces cerevisiae
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.3.4
Saccharomyces cerevisiae
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
3.1.3.4
PtA fusion affinity purification
Saccharomyces cerevisiae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.4
phosphatidic acid + H2O
-
716758
Saccharomyces cerevisiae
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
3.1.3.4
additional information
dephosphorylation of lipin Pah1p by the Nem1p-Spo7p complex enables the amphipathic helix to anchor Pah1p onto the nuclear/endoplasmic reticulum membrane allowing the production of diacylglycerol for lipid biosynthesis
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.1.3.4
0.43
-
phosphatidic acid
wild type enzyme, pH and temperature not specified in the publication
Saccharomyces cerevisiae
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.4
membrane
recruitment of the yeast lipin (Pah1p) is regulated by PA levels onto the nuclear/endoplasmic reticulum membrane. Recruitment requires the transmembrane protein phosphatase complex Nem1p-Spo7p
Saccharomyces cerevisiae
16020
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
Mg2+
dependent on
Saccharomyces cerevisiae
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.3.4
PtA fusion affinity purification
Saccharomyces cerevisiae
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
phosphatidic acid + H2O
-
716758
Saccharomyces cerevisiae
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
General Information
EC Number
General Information
Commentary
Organism
3.1.3.4
physiological function
lipins are essential regulators of fat metabolism, adipogenesis, and organelle biogenesis
Saccharomyces cerevisiae
General Information (protein specific)
EC Number
General Information
Commentary
Organism
3.1.3.4
physiological function
lipins are essential regulators of fat metabolism, adipogenesis, and organelle biogenesis
Saccharomyces cerevisiae