BRENDA - Enzyme Database

Arabidopsis lipins mediate eukaryotic pathway of lipid metabolism and cope critically with phosphate starvation

Nakamura, Y.; Koizumi, R.; Shui, G.; Shimojima, M.; Wenk, M.R.; Ito, T.; Ohta, H.; Proc. Natl. Acad. Sci. USA 106, 20978-20983 (2009)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
3.1.3.4
full-length coding sequence of PAH1 and PAH2 cloned into the pDO105 vector at NotI/MluI sites for PAH1 and NotI/PstI sites for PAH2. Vector constructs introduced into a Saccharomyces cerevisiae DELTAdpp1DELTAlpp1DELTApah1 mutant. Transgenic pah1pah2 plants that harbor either 35S::PAH1-GFP or 35S::PAH2-GFP transgenes
Arabidopsis thaliana
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.4
soluble
PAH1 and PAH2
Arabidopsis thaliana
-
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
Mg2+
depends on
Arabidopsis thaliana
3.1.3.4
Mg2+
depends on
Saccharomyces cerevisiae
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.3.4
101000
-
PAH1 and PAH2, calculated from sequence
Arabidopsis thaliana
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.3.4
Arabidopsis thaliana
-
-
-
3.1.3.4
Saccharomyces cerevisiae
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.3.4
leaf
-
Arabidopsis thaliana
-
3.1.3.4
rosette leaf
-
Arabidopsis thaliana
-
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
both PAH1 and PAH2 have two domains, the amino-terminal lipin and carboxy-terminal lipin domains. PAH1 and PAH2 may supply diacylglycerol as a substrate of galactolipid synthesis, and phosphatidic acid hydrolyzed by PAH1 and PAH2 may be derived from phosphatidylcholine and phosphatidylethanolamine
710418
Arabidopsis thaliana
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.3.4
full-length coding sequence of PAH1 and PAH2 cloned into the pDO105 vector at NotI/MluI sites for PAH1 and NotI/PstI sites for PAH2. Vector constructs introduced into a Saccharomyces cerevisiae DELTAdpp1DELTAlpp1DELTApah1 mutant. Transgenic pah1pah2 plants that harbor either 35S::PAH1-GFP or 35S::PAH2-GFP transgenes
Arabidopsis thaliana
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.4
soluble
PAH1 and PAH2
Arabidopsis thaliana
-
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
Mg2+
depends on
Arabidopsis thaliana
3.1.3.4
Mg2+
depends on
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.3.4
101000
-
PAH1 and PAH2, calculated from sequence
Arabidopsis thaliana
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.3.4
leaf
-
Arabidopsis thaliana
-
3.1.3.4
rosette leaf
-
Arabidopsis thaliana
-
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
both PAH1 and PAH2 have two domains, the amino-terminal lipin and carboxy-terminal lipin domains. PAH1 and PAH2 may supply diacylglycerol as a substrate of galactolipid synthesis, and phosphatidic acid hydrolyzed by PAH1 and PAH2 may be derived from phosphatidylcholine and phosphatidylethanolamine
710418
Arabidopsis thaliana
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
Expression
EC Number
Organism
Commentary
Expression
3.1.3.4
Arabidopsis thaliana
homozygous T-DNA-tagged mutants of PAH1 and PAH2 do not express their respective full-length mRNAs
down
General Information
EC Number
General Information
Commentary
Organism
3.1.3.4
malfunction
double mutant pah1pah2 plants have decreased phosphatidic acid hydrolysis, thus affecting the eukaryotic pathway of galactolipid synthesis. Upon phosphate starvation, pah1pah2 plants are severely impaired in growth and membrane lipid remodeling. PAP activity in the supernatant fraction of pah1pah2 mutant leaves is decreased by approximately 40% as compared to that in wild-type leaves. Defect in PAP activity in vivo in rosette leaves of pah1pah2 mutants. Relative amount of phosphatidic acid increases to 1.61fold in pah1pah2 double mutants as compared to the wild-type. 26% increase in phosphatidic acid levels in pah1pah2 plants as compared to wild-type plants. The transgenic plants (35S::PAH1-GFP, pah1pah2 and 35S::PAH2-GFP, pah1pah2) recover the phenotype observed in pah1pah2 mutant. Endoplasmic reticulum-localized eukaryotic pathway of membrane lipid metabolism is compromised in pah1pah2 double mutants
Arabidopsis thaliana
3.1.3.4
malfunction
yeast DELTAdpp1DELTAlpp1DELTApah1 mutant is complemented by Arabidopsis phosphatidate phosphatases PAH1 and PAH2 in vivo
Saccharomyces cerevisiae
3.1.3.4
physiological function
PAH1 and PAH2 are the phosphatidate phosphatase responsible for the eukaryotic pathway of galactolipid synthesis. Membrane lipid remodeling mediated by these two enzymes is an essential adaptation mechanism to cope with phosphate starvation. Complements yeast DELTAdpp1DELTAlpp1DELTApah1 in vivo
Arabidopsis thaliana
General Information (protein specific)
EC Number
General Information
Commentary
Organism
3.1.3.4
malfunction
double mutant pah1pah2 plants have decreased phosphatidic acid hydrolysis, thus affecting the eukaryotic pathway of galactolipid synthesis. Upon phosphate starvation, pah1pah2 plants are severely impaired in growth and membrane lipid remodeling. PAP activity in the supernatant fraction of pah1pah2 mutant leaves is decreased by approximately 40% as compared to that in wild-type leaves. Defect in PAP activity in vivo in rosette leaves of pah1pah2 mutants. Relative amount of phosphatidic acid increases to 1.61fold in pah1pah2 double mutants as compared to the wild-type. 26% increase in phosphatidic acid levels in pah1pah2 plants as compared to wild-type plants. The transgenic plants (35S::PAH1-GFP, pah1pah2 and 35S::PAH2-GFP, pah1pah2) recover the phenotype observed in pah1pah2 mutant. Endoplasmic reticulum-localized eukaryotic pathway of membrane lipid metabolism is compromised in pah1pah2 double mutants
Arabidopsis thaliana
3.1.3.4
malfunction
yeast DELTAdpp1DELTAlpp1DELTApah1 mutant is complemented by Arabidopsis phosphatidate phosphatases PAH1 and PAH2 in vivo
Saccharomyces cerevisiae
3.1.3.4
physiological function
PAH1 and PAH2 are the phosphatidate phosphatase responsible for the eukaryotic pathway of galactolipid synthesis. Membrane lipid remodeling mediated by these two enzymes is an essential adaptation mechanism to cope with phosphate starvation. Complements yeast DELTAdpp1DELTAlpp1DELTApah1 in vivo
Arabidopsis thaliana
Expression (protein specific)
EC Number
Organism
Commentary
Expression
3.1.3.4
Arabidopsis thaliana
homozygous T-DNA-tagged mutants of PAH1 and PAH2 do not express their respective full-length mRNAs
down