In enzymology, a nickel-transporting ATPase (EC 3.6.3.24) is an enzyme that catalyzes the chemical reaction
| nickel-transporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.3.24 | ||||||||
| 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 | ||||||||
| |||||||||
- ATP + H2O + Ni2+out ADP + phosphate + Ni2+in
The 3 substrates of this enzyme are ATP, H2O, and Ni2+, whereas its 3 products are ADP, phosphate, and Ni2+.
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 (nickel-importing).
Structural studies
editAs of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1ZLQ and 2NOO.
References
edit- Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH (1995). "Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases". Res. Microbiol. 146 (4): 271–8. doi:10.1016/0923-2508(96)81050-3. PMID 7569321.
- Hendricks JK, Mobley HL (1997). "Helicobacter pylori ABC transporter: effect of allelic exchange mutagenesis on urease activity". J. Bacteriol. 179 (18): 5892–902. doi:10.1128/jb.179.18.5892-5902.1997. PMC 179482. PMID 9294450.
- Saier MH (1998). "Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya". Adv. Microb. Physiol. Advances in Microbial Physiology. 40: 81–136. doi:10.1016/S0065-2911(08)60130-7. ISBN 9780120277407. PMID 9889977.
- Griffiths JK; Sansom CE. "The Transporter Factsbook, Academic Press, San Diego, 1998".
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