BRENDA - Enzyme Database

Roles of phosphatidate phosphatase enzymes in lipid metabolism

Carman, G.M.; Han, G.S.; Trends Biochem. Sci. 31, 694-699 (2006)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
3.1.3.4
additional information
pah1? mutants show a temperature sensitivity phenotype
Saccharomyces cerevisiae
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.3.4
bromoenol lactone
selective inhibition of PAP1
Saccharomyces cerevisiae
3.1.3.4
diacylglycerol
DPP1-encoded PAP2 enzyme is inhibited by CDP-DAG
Saccharomyces cerevisiae
3.1.3.4
NEM
the yeast DPP1-encoded PAP2 activity is insensitive to NEM, whereas LPP1-encoded PAP2 activity is sensitive to NEM
Saccharomyces cerevisiae
3.1.3.4
Zn2+
PAP2 activity is also inhibited by Zn2+ ions in a mechanism that involves the formation of DGPP-Zn2+ complexes
Saccharomyces cerevisiae
3.1.3.81
diacylglycerol
DPP1-encoded PAP2 enzyme is inhibited by CDP-DAG
Saccharomyces cerevisiae
3.1.3.81
additional information
Dpp1p, DPP1-encoded PAP2 activity, is NEM-insensitive
Saccharomyces cerevisiae
3.1.3.81
Zn2+
DPP1-encoded PAP2 activity is inhibited by Zn2+ ions in a mechanism that involves the formation of DGPP-Zn2+ complexes
Saccharomyces cerevisiae
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.4
cytosol
isozyme PAP1
Saccharomyces cerevisiae
5829
-
3.1.3.4
membrane
isozyme PAP1, PAP2s are integral membrane proteins
Saccharomyces cerevisiae
16020
-
3.1.3.81
Golgi membrane
-
Saccharomyces cerevisiae
139
-
3.1.3.81
membrane
an integral membrane protein with six transmembrane spanning regions
Saccharomyces cerevisiae
16020
-
3.1.3.81
vacuolar membrane
-
Saccharomyces cerevisiae
5774
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
additional information
Lpp1p contains ten cysteine residues, whereas Dpp1p and Pah1p contain only three
Saccharomyces cerevisiae
3.1.3.81
additional information
no requirement for Mg2+
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
phosphatidic acid + H2O
Saccharomyces cerevisiae
PAP activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signaling molecules that are related to phosphatidate, isozyme PAP1 plays a role in the transcriptional regulation of phospholipid synthesis, overview
1,2-diacylglycerol + phosphate
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae
the bifunctional Dpp1p catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
phosphatidate + phosphate
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.3.4
Saccharomyces cerevisiae
-
isozymes PAP1 and PAP2, encoded by genes PAH1, formerly known as SMP2, and DPP1 and LPP1, respectively
-
3.1.3.81
Saccharomyces cerevisiae
-
gene DPP1
-
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
-
682952
Saccharomyces cerevisiae
1,2-diacylglycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
PAP activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signaling molecules that are related to phosphatidate, isozyme PAP1 plays a role in the transcriptional regulation of phospholipid synthesis, overview
682952
Saccharomyces cerevisiae
1,2-diacylglycerol + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
the bifunctional Dpp1p catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
682952
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
3.1.3.4
More
PAP1 enzyme has a DxDxT catalytic motif within a haloacid dehalogenase- like domain, the DPP1-and LPP1-encoded PAP2 enzymes contain a three-domain lipid phosphatase motif that is localized to the hydrophilic surface of the membrane
Saccharomyces cerevisiae
3.1.3.81
More
Dpp1p contains three cysteine residues, the DPP1-encoded PAP2 enzyme contains a three-domain lipid phosphatase motif that is localized to the hydrophilic surface of the membrane
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
3.1.3.4
additional information
pah1? mutants show a temperature sensitivity phenotype
Saccharomyces cerevisiae
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.3.4
bromoenol lactone
selective inhibition of PAP1
Saccharomyces cerevisiae
3.1.3.4
diacylglycerol
DPP1-encoded PAP2 enzyme is inhibited by CDP-DAG
Saccharomyces cerevisiae
3.1.3.4
NEM
the yeast DPP1-encoded PAP2 activity is insensitive to NEM, whereas LPP1-encoded PAP2 activity is sensitive to NEM
Saccharomyces cerevisiae
3.1.3.4
Zn2+
PAP2 activity is also inhibited by Zn2+ ions in a mechanism that involves the formation of DGPP-Zn2+ complexes
Saccharomyces cerevisiae
3.1.3.81
diacylglycerol
DPP1-encoded PAP2 enzyme is inhibited by CDP-DAG
Saccharomyces cerevisiae
3.1.3.81
additional information
Dpp1p, DPP1-encoded PAP2 activity, is NEM-insensitive
Saccharomyces cerevisiae
3.1.3.81
Zn2+
DPP1-encoded PAP2 activity is inhibited by Zn2+ ions in a mechanism that involves the formation of DGPP-Zn2+ complexes
Saccharomyces cerevisiae
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.4
cytosol
isozyme PAP1
Saccharomyces cerevisiae
5829
-
3.1.3.4
membrane
isozyme PAP1, PAP2s are integral membrane proteins
Saccharomyces cerevisiae
16020
-
3.1.3.81
Golgi membrane
-
Saccharomyces cerevisiae
139
-
3.1.3.81
membrane
an integral membrane protein with six transmembrane spanning regions
Saccharomyces cerevisiae
16020
-
3.1.3.81
vacuolar membrane
-
Saccharomyces cerevisiae
5774
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
additional information
Lpp1p contains ten cysteine residues, whereas Dpp1p and Pah1p contain only three
Saccharomyces cerevisiae
3.1.3.81
additional information
no requirement for Mg2+
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
phosphatidic acid + H2O
Saccharomyces cerevisiae
PAP activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signaling molecules that are related to phosphatidate, isozyme PAP1 plays a role in the transcriptional regulation of phospholipid synthesis, overview
1,2-diacylglycerol + phosphate
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae
the bifunctional Dpp1p catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
phosphatidate + phosphate
-
-
?
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
-
682952
Saccharomyces cerevisiae
1,2-diacylglycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
PAP activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signaling molecules that are related to phosphatidate, isozyme PAP1 plays a role in the transcriptional regulation of phospholipid synthesis, overview
682952
Saccharomyces cerevisiae
1,2-diacylglycerol + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
the bifunctional Dpp1p catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
682952
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
3.1.3.4
More
PAP1 enzyme has a DxDxT catalytic motif within a haloacid dehalogenase- like domain, the DPP1-and LPP1-encoded PAP2 enzymes contain a three-domain lipid phosphatase motif that is localized to the hydrophilic surface of the membrane
Saccharomyces cerevisiae
3.1.3.81
More
Dpp1p contains three cysteine residues, the DPP1-encoded PAP2 enzyme contains a three-domain lipid phosphatase motif that is localized to the hydrophilic surface of the membrane
Saccharomyces cerevisiae