In enzymology, a polyamine-transporting ATPase (EC 3.6.3.31) is an enzyme that catalyzes the chemical reaction
| polyamine-transporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.3.31 | ||||||||
| 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 + polyamineout ADP + phosphate + polyaminein
The 3 substrates of this enzyme are ATP, H2O, and polyamine, whereas its 3 products are ADP, phosphate, and polyamine.
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 (polyamine-importing). This enzyme participates in abc transporters - general.
References
edit- Kashiwagi K, Miyamoto S, Nukui E, Kobayashi H, Igarashi K (1993). "Functions of potA and potD proteins in spermidine-preferential uptake system in Escherichia coli". J. Biol. Chem. 268 (26): 19358–63. PMID 8366082.
- Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr (1995). "Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases". Res. Microbiol. 146 (4): 271–278. doi:10.1016/0923-2508(96)81050-3. PMID 7569321.
- Saier MH Jr (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 978-0-12-027740-7. PMID 9889977.
