Nonpolar-amino-acid-transporting ATPase
| nonpolar-amino acid-transporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.3.22 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a nonpolar-amino-acid-transporting ATPase (EC 3.6.3.22) is an enzyme that catalyzes the chemical reaction
- ATP + H2O + nonpolar amino acidout ADP + phosphate + nonpolar amino acidin
The 3 substrates of this enzyme are ATP, H2O, and nonpolar amino acid, whereas its 3 products are ADP, phosphate, and nonpolar amino acid.
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 (nonpolar-amino-acid-transporting).
References
- 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). "Advances in Microbial Physiology Volume 40; Chapter - 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.
- Griffiths JK; Sansom CE. "The Transporter Factsbook, Academic Press, San Diego, 1998".
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