Member database | SUPERFAMILY |
SUPERFAMILY type | homologous superfamily |
Description Imported from IPR036938
This entry represents type 2 phosphatidic acid phosphatase (PAP2;
3.1.3.4) enzymes, such as phosphatidylglycerophosphatase B
3.1.3.27 from Escherichia coli. PAP2 enzymes have a core structure consisting of a 5-helical bundle, where the beginning of the third helix binds the cofactor
[2]. PAP2 enzymes catalyse the dephosphorylation of phosphatidate, yielding diacylglycerol and inorganic phosphate
[1]. In eukaryotic cells, 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-signalling molecules that are related to phosphatidate.
Other related enzymes have a similar core structure, including haloperoxidases such as bromoperoxidase (contains one core bundle, but forms a dimer), chloroperoxidases (contains two core bundles arranged as in other family dimers), bacitracin transport permease from Bacillus licheniformis, glucose-6-phosphatase from rat. The vanadium-dependent haloperoxidases exclusively catalyse the oxidation of halides, and act as histidine phosphatases, using histidine for the nucleophilic attack in the first step of the reaction
[3]. Amino acid residues involved in binding phosphate/vanadate are conserved between the two families, supporting a proposal that vanadium passes through a tetrahedral intermediate during the reaction mechanism.
References Imported from IPR036938
1.Roles of phosphatidate phosphatase enzymes in lipid metabolism. Carman GM, Han GS. Trends Biochem. Sci. 31, 694-9, (2006). View articlePMID: 17079146
2.X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate. Ishikawa K, Mihara Y, Gondoh K, Suzuki E, Asano Y. EMBO J. 19, 2412-23, (2000). View articlePMID: 10835340
3.Structural and functional comparisons between vanadium haloperoxidase and acid phosphatase enzymes. Littlechild J, Garcia-Rodriguez E, Dalby A, Isupov M. J. Mol. Recognit. 15, 291-6, (2002). View articlePMID: 12447906