Phosphatidate phosphatase | |||||||||
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Identifiers | |||||||||
EC number | 3.1.3.4 | ||||||||
CAS number | 9025-77-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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Search | |
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PMC | articles |
PubMed | articles |
NCBI | proteins |
Phosphatidate phosphatase (PAP) (EC 3.1.3.4) is a key regulatory enzyme in lipid metabolism, catalyzing the conversion of phosphatidate to diacylglycerol. The two substrates of PAP are phosphatidate and H2O, and its two products are diacylglycerol and phosphate, as shown here.
The reverse reaction is catalyzed by the enzyme diacylglycerol kinase (DGK or DAGK), which replaces the hydroxyl group on diacylgylcerol with a phosphate from ATP, generating ADP in the process. While ATP is used by DGK in mammalian cells, yeast cells tend to use CTP as the high-energy phosphate donor instead. Mechanistically speaking, this has no effect on the overall reaction.
In yeast, the forward direction is -dependent, while the reverse direction is -dependent. PAP1, a cytosolic phosphatidate phosphatase found in the lung, is also -dependent, but PAP2, a six-transmembrane-domain integral protein found in the plasma membrane, is not.