Oligopeptide-transporting ATPase
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| oligopeptide-transporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.3.23 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an oligopeptide-transporting ATPase (EC 3.6.3.23) is an enzyme that catalyzes the chemical reaction
- ATP + H2O + oligopeptide(out) ADP + phosphate + oligopeptide(in)
The 3 substrates of this enzyme are ATP, H2O, and oligopeptide, whereas its 3 products are ADP, phosphate, and oligopeptide.
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 (oligopeptide-importing). This enzyme is also called oligopeptide permease.
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). "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".
{{cite journal}}: Cite journal requires|journal=(help) - Pearce SR, Mimmack ML, Gallagher MP, Gileadi U, Hyde SC, Higgins CF (1992). "Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium". Mol. Microbiol. 6 (1): 47–57. doi:10.1111/j.1365-2958.1992.tb00836.x. PMID 1738314. S2CID 1660114.
