| chloride-transporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.3.11 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a Cl-transporting ATPase (EC 3.6.3.11) is an enzyme that catalyzes the chemical reaction
- ATP + H2O + Cl−out ADP + phosphate + Cl−in
The 3 substrates of this enzyme are ATP, H2O, and Cl−, whereas its 3 products are ADP, phosphate, and Cl−.
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 (Cl−-importing). Other names in common use include Cl−-translocating ATPase, and Cl−-motive ATPase.
References
- Ohhashi T, Katsu T, Ikeda M (1992). "Improvement of reconstitution of the Cl−-translocating ATPase isolated from Acetabularia acetabulum into liposomes and several anion pump characteristics". Biochim. Biophys. Acta. 1106 (1): 165–70. doi:10.1016/0005-2736(92)90235-E. PMID 1533790.
- Gerencser GA, Purushotham KR (1996). "Reconstituted Cl− pump protein: a novel ion (Cl−)-motive ATPase". J. Bioenerg. Biomembr. 28 (6): 459–69. doi:10.1007/BF02110436. PMID 8953378.
- Inagaki C, Hara M, Zeng XT (1996). "A Cl− pump in rat brain neurons". J. Exp. Zool. 275 (4): 262–8. doi:10.1002/(SICI)1097-010X(19960701)275:4<262::AID-JEZ3>3.0.CO;2-N. PMID 8759922.
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