Biology:Peptide-transporting ATPase
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Short description: Class of enzymes
| peptide-transporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.3.43 | ||||||||
| 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, a peptide-transporting ATPase (EC 3.6.3.43) is an enzyme that catalyzes the chemical reaction
- ATP + H2O + peptidein [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate + peptideout
The 3 substrates of this enzyme are ATP, H2O, and peptide, whereas its 3 products are ADP, phosphate, and peptide.
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 (peptide-exporting).
References
- "Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis ATCC 6633". Appl. Environ. Microbiol. 60 (8): 2793–801. 1994. PMID 8085823.
- JJ; Roelse, J; Howard, JC; Butcher, GW; Hämmerling, GJ; Neefjes, JJ (1994). "Selectivity of MHC-encoded peptide transporters from human, mouse and rat". Nature 367 (6464): 648–51. doi:10.1038/367648a0. PMID 8107849.
- "Protein secretion by Gram-negative bacterial ABC exporters-a review". Gene 192 (1): 7–11. 1997. doi:10.1016/S0378-1119(96)00829-3. PMID 9224868.
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