Arsenite-transporting ATPase

From Wikipedia, the free encyclopedia

In enzymology, an arsenite-transporting ATPase (EC 3.6.3.16) is an enzyme that catalyzes the chemical reaction

ATP + H₂O + arsenitein $\rightleftharpoons$ ADP + phosphate + arseniteout

The 3 substrates of this enzyme are ATP, H₂O, and arsenite, whereas its 3 products are ADP, phosphate, and arsenite.

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 (arsenite-exporting).

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1IHU, 1II0, and 1II9.

[edit] References

IUBMB entry for 3.6.3.16
BRENDA references for 3.6.3.16 (Recommended.)
PubMed references for 3.6.3.16
PubMed Central references for 3.6.3.16
Google Scholar references for 3.6.3.16
Silver S, Misra TK, Laddaga RA (1989). "DNA sequence analysis of bacterial toxic heavy metal resistances". Biol. Trace. Elem. Res. 21: 145–63. PMID 2484581.
Rosen BP, Weigel U, Monticello RA, Edwards BP (1991). "Molecular analysis of an anion pump: purification of the ArsC protein". Arch. Biochem. Biophys. 284: 381–5. doi:10.1016/0003-9861(91)90312-7. PMID 1703401.
Rosen BP, Weigel U, Monticello RA, Edwards BP (1991). "Molecular analysis of an anion pump: purification of the ArsC protein". Arch. Biochem. Biophys. 284: 381–5. doi:10.1016/0003-9861(91)90312-7. PMID 1703401.
Zhou T, Rosen BP, Gatti DL (Pt 4). "Crystallization and preliminary x-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773". Acta. Crystallogr. D. Biol. Crystallogr. 55: 921–4. doi:10.1107/S0907444999000256. PMID 10089335.