Cd2+-exporting ATPase
| cadmium-exporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.3.3 | ||||||||
| 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 Cd2+-exporting ATPase (EC 3.6.3.3) is an enzyme that catalyzes the chemical reaction
- ATP + H2O + Cd2+in ADP + phosphate + Cd2+out
The 3 substrates of this enzyme are ATP, H2O, and Cd2+, whereas its 3 products are ADP, phosphate, and Cd2+.
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 (Cd2+-exporting).
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1MWY, 1MWZ, 2AJ0, and 2AJ1.
References
- Silver S, Ji G (1994). "Newer systems for bacterial resistances to toxic heavy metals". Environ. Health Perspect. 102 (Suppl. 3): 107&ndash, 13. PMC 1567394. PMID 7843081.
- Tsai KJ, Linet AL (1993). "Formation of a phosphorylated enzyme intermediate by the cadA Cd(2+)-ATPase". Arch. Biochem. Biophys. 305 (2): 267&ndash, 70. doi:10.1006/abbi.1993.1421. PMID 8373163.
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