In enzymology, a Na+-transporting two-sector ATPase (EC 3.6.3.15) is an enzyme that catalyzes the chemical reaction
| sodium-transporting ATPase, rotational mechanism | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.3.15 | ||||||||
| 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 | ||||||||
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- ATP + H2O ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate.
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 (Na+-transporting).
References
edit- Solioz M, Davies K (1994). "Operon of vacuolar-type Na+-ATPase of Enterococcus hirae". J. Biol. Chem. 269 (13): 9453–9. PMID 8144530.
- Takase K, Kakinuma S, Yamato I, Konishi K, Igarashi K, Kakinuma Y (1994). "Sequencing and characterization of the ntp gene cluster for vacuolar-type Na+-translocating ATPase of Enterococcus hirae". J. Biol. Chem. 269 (15): 11037–44. PMID 8157629.
- Rahlfs S, Muller V (1997). "Sequence of subunit c of the Na(+)-translocating F1F0 ATPase of Acetobacterium woodii: proposal for determinants of Na+ specificity as revealed by sequence comparisons". FEBS Lett. 404 (2–3): 269–71. doi:10.1016/S0014-5793(97)00088-4. PMID 9119076.
