Biology:Zn2+-exporting ATPase
| zinc-exporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.3.5 | ||||||||
| 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 Zn2+-exporting ATPase (EC 3.6.3.5) is an enzyme that catalyzes the chemical reaction
- ATP + H2O + Zn2+in [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate + Zn2+out
The 3 substrates of this enzyme are ATP, H2O, and Zn2+, whereas its 3 products are ADP, phosphate, and Zn2+.
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 (Zn2+-exporting). Other names in common use include Zn(II)-translocating P-type ATPase, P1B-type ATPase, and AtHMA4 (the A. thaliana protein).
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1MWY and 1MWZ. Moreover, nanobodies have recently been raised against a zinc-transporting ATPase (ZntA) which are able to bind and inhibit the ATPase activity, showing potential for further structural studies.[1]
References
- ↑ Longhin, Elena; Grønberg, Christina; Hu, Qiaoxia; Duelli, Annette; Andersen, Kasper; Laursen, Nick; Gourdon, Pontus (7 November 2018). "Isolation and Characterization of Nanobodies against a Zinc-Transporting P-Type ATPase". Antibodies 7 (4): 39. doi:10.3390/antib7040039. PMID 31544889.
- "Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase". Mol. Microbiol. 25 (5): 883–91. 1997. doi:10.1111/j.1365-2958.1997.mmi518.x. PMID 9364914.
- "The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14326–31. 1997. doi:10.1073/pnas.94.26.14326. PMID 9405611. Bibcode: 1997PNAS...9414326R.
- "Pb(II)-translocating P-type ATPases". J. Biol. Chem. 273 (49): 32614–7. 1998. doi:10.1074/jbc.273.49.32614. PMID 9830000.
- "The plant P1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels". FEBS Lett. 579 (3): 783–91. 2005. doi:10.1016/j.febslet.2004.12.040. PMID 15670847.
- "Arabidopsis HMA2, a Divalent Heavy Metal-Transporting PIB-Type ATPase, Is Involved in Cytoplasmic Zn2+ Homeostasis". Plant Physiol. 136 (3): 3712–23. 2004. doi:10.1104/pp.104.046292. PMID 15475410.
 |  |
