K+-transporting ATPase
From Wikipedia, the free encyclopedia
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 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.
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[edit] 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.
[edit] References
- IUBMB entry for 3.6.3.12
- BRENDA references for 3.6.3.12 (Recommended.)
- PubMed references for 3.6.3.12
- PubMed Central references for 3.6.3.12
- Google Scholar references for 3.6.3.12
- Siebers A, Altendorf K (1989). "Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli". J. Biol. Chem. 264: 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: 77–84. PMID 9858692.