K+-transporting ATPase
| potassium-transporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.3.12 | ||||||||
| 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 K+-transporting ATPase (EC 3.6.3.12) is an enzyme that catalyzes the chemical reaction
- ATP + H2O + K+out ⇌ ADP + phosphate + K+in
The 3 substrates of this enzyme are ATP, H2O, and K+, whereas its 3 products are ADP, phosphate, and K+.
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 (K+-importing). Other names in common use include K+-translocating Kdp-ATPase, and multi-subunit K+-transport ATPase. This enzyme participates in two-component system - general.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1SVJ, 1U7Q, 2A00, and 2A29.
References
- Siebers A, Altendorf K (1989). "Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli". J. Biol. Chem. 264 (10): 5831–8. PMID 2522440.
- Gassel M, Siebers A, Epstein W, Altendorf K (1998). "Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli". Biochim. Biophys. Acta. 1415 (1): 77–84. doi:10.1016/S0005-2736(98)00179-5. PMID 9858692.
