In enzymology, a lipopolysaccharide-transporting ATPase (EC 3.6.3.39) is an enzyme that catalyzes the chemical reaction
| lipopolysaccharide-transporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.3.39 | ||||||||
| 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 | ||||||||
| |||||||||
- ATP + H2O + lipopolysaccharidein ADP + phosphate + lipopolysaccharideout
The 3 substrates of this enzyme are ATP, H2O, and lipopolysaccharide, whereas its 3 products are ADP, phosphate, and lipopolysaccharide.
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 (lipopolysaccharide-exporting).
References
edit- Fath MJ, Kolter R (1993). "ABC transporters: bacterial exporters". Microbiol. Rev. 57 (4): 995–1017. doi:10.1128/mmbr.57.4.995-1017.1993. PMC 372944. PMID 8302219.
- Van Montagu M, Holsters M (1996). "Role of nodl and nodJ in lipo-chitooligosaccharide secretion in Azorhizobium caulinodans and Escherichia coli". Mol. Microbiol. 20 (5): 993–1000. doi:10.1111/j.1365-2958.1996.tb02540.x. PMID 8809752.
- Paulsen IT, Beness AM, Saier MH. "Computer-based analyses of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria". Microbiology. 143 (8): 2685–99. doi:10.1099/00221287-143-8-2685. PMID 9274022.
- Saier MH Jr (1998). "Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya". Adv. Microb. Physiol. 40: 81–136. doi:10.1016/S0065-2911(08)60130-7. PMID 9889977.
