In enzymology, a sulfate-transporting ATPase (EC 3.6.3.25) is an enzyme that catalyzes the chemical reaction
sulfate transmembrane-transporting ATPase | |||||||||
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Identifiers | |||||||||
EC no. | 3.6.3.25 | ||||||||
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 + sulfateout ADP + phosphate + sulfatein
The 3 substrates of this enzyme are ATP, H2O, and sulfate, whereas its 3 products are ADP, phosphate, and sulfate.
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 (sulfate-importing). This enzyme participates in abc transporters - general.
References
edit- Sirko A, Zatyka M, Sadowy E, Hulanicka D (1995). "Sulfate and thiosulfate transport in Escherichia coli K-12: evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins". J. Bacteriol. 177 (14): 4134–6. PMC 177147. PMID 7608089.
- 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 978-0-12-027740-7. PMID 9889977.