释义 |
- Structural studies
- References
{{enzyme | Name = zinc-exporting ATPase | EC_number = 3.6.3.5 | CAS_number = | IUBMB_EC_number = 3/6/3/5 | GO_code = 0016463 | image = | width = | caption = }}In enzymology, a Zn2+-exporting ATPase ({{EC number|3.6.3.5}}) is an enzyme that catalyzes the chemical reaction ATP + H2O + Zn2+in 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 {{PDB link|1MWY}} and {{PDB link|1MWZ}}. References - {{cite journal | vauthors = Beard SJ, Hashim R, Membrillo-Hernandez J, Hughes MN, Poole RK | year = 1997 | title = Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase | journal = Mol. Microbiol. | volume = 25 | pages = 883–91 | pmid = 9364914 | doi = 10.1111/j.1365-2958.1997.mmi518.x | issue = 5 }}
- {{cite journal | vauthors = Rensing C, Mitra B, Rosen BP | year = 1997 | title = The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 94 | pages = 14326–31 | pmid = 9405611 | doi = 10.1073/pnas.94.26.14326 | issue = 26 | pmc = 24962 }}
- {{cite journal | vauthors = Rensing C, Sun Y, Mitra B, Rosen BP | year = 1998 | title = Pb(II)-translocating P-type ATPases | journal = J. Biol. Chem. | volume = 273 | pages = 32614–7 | pmid = 9830000 | doi = 10.1074/jbc.273.49.32614 | issue = 49 }}
- {{cite journal | vauthors = Krijger GC, Williams LE | year = 2005 | title = The plant P1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels | journal = FEBS Lett. | volume = 579 | pages = 783–91 | pmid = 15670847 | doi = 10.1016/j.febslet.2004.12.040 | issue = 3 }}
- {{cite journal | vauthors = Eren E, Arguello JM | year = 2004 | title = Arabidopsis HMA2, a Divalent Heavy Metal-Transporting PIB-Type ATPase, Is Involved in Cytoplasmic Zn2+ Homeostasis | journal = Plant Physiol. | volume = 136 | pages = 3712–23 | pmid = 15475410 | doi = 10.1104/pp.104.046292 | issue = 3 | pmc = 527169 }}
{{Acid anhydride hydrolases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{3.6-enzyme-stub}} 2 : EC 3.6.3|Enzymes of known structure |