In enzymology, a phospholipid-translocating ATPase (EC 3.6.3.1) is an enzyme that catalyzes the chemical reaction
| phospholipid-translocating ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.3.1 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
- ATP + H2O + phospholipid in ADP + phosphate + phospholipid out
The 3 substrates of this enzyme are ATP, H2O, and phospholipid, whereas its 3 products are ADP, phosphate, and phospholipid.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (phospholipid-flipping). Other names in common use include Mg2+-ATPase, flippase, and aminophospholipid-transporting ATPase.
References
edit- Morris MB, Auland ME, Xu YH, Roufogalis BD (1993). "Characterization of the Mg(2+)-ATPase activity of the human erythrocyte membrane". Biochem. Mol. Biol. Int. 31 (5): 823–32. PMID 8136700.
- Vermeulen WP, Briede JJ, Roelofsen B (1996). "Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity". Mol. Membr. Biol. 13 (2): 95–102. doi:10.3109/09687689609160582. PMID 8839453.
- Suzuki H, Kamakura M, Morii M, Takeguchi N (1997). "The phospholipid flippase activity of gastric vesicles". J. Biol. Chem. 272 (16): 10429–34. doi:10.1074/jbc.272.16.10429. PMID 9099684.
- Auland ME, Roufogalis BD, Devaux PF, Zachowski A (1994). "Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes". Proc. Natl. Acad. Sci. U.S.A. 91 (23): 10938–42. doi:10.1073/pnas.91.23.10938. PMC 45141. PMID 7971987.
