In enzymology, a phosphonate-transporting ATPase (EC 3.6.3.28) is an enzyme that catalyzes the chemical reaction
phosphonate transmembrane-transporting ATPase | |||||||||
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Identifiers | |||||||||
EC no. | 3.6.3.28 | ||||||||
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 | ||||||||
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- ATP + H2O + phosphonateout ADP + phosphate + phosphonatein
The 3 substrates of this enzyme are ATP, H2O, and phosphonate, whereas its 3 products are ADP, phosphate, and phosphonate.
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 (phosphonate-transporting).
References
edit- Wanner BL, Metcalf WW (1992). "Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation". FEMS Microbiol. Lett. 79 (1–3): 133–9. doi:10.1111/j.1574-6968.1992.tb14031.x. PMID 1335942.
- 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.
- 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 9780120277407. PMID 9889977.
- Griffiths JK; Sansom CE. "The Transporter Factsbook, Academic Press, San Diego, 1998".
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