EC Number   |
Reaction |
Reference |
|---|
   7.6.2.2 | ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] |
- |
- |
| 7.6.2.2 | ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] |
ABC-type, ATP-binding cassette-type, ATPase, characterized by the presence of two similar ATP-binding domains, does not undergo phosphorylation during the transport process, enzymes of Gram-positive bacteria and eukaryotic cells that export a number of drugs, with unusual specificity, covering various groups of unrelated substances, while ignoring some that are closely related structurally, several distinct enzymes may be present in a single eukaryotic cell, many of them transport glutathione conjugates with drugs, some also show some flippase, Mg2+-ATPase, EC 3.6.3.1, activity |
658168 |
| 7.6.2.2 | ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] |
mechanism |
657840, 657931 |
| 7.6.2.2 | ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] |
P-gp mediated-transport mechanism, overview |
697006 |
| 7.6.2.2 | ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] |
positive cooperativity mechanism |
658086 |
| 7.6.2.2 | ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] |
the high to low affinity switch in the transport substrate binding site is due to the formation of the E-S reaction intermediate of the ATPase reaction. The posthydrolysis E-P state continues to have low affinity for substrate, suggesting that conformational changes that form the E-S complex are coupled to the conformational change at the transport substrate site to do mechanical work. The formation of E-S reaction intermediate during a single turnover of the catalytic cycle appears to provide the initial power stroke for movement of drug substrate from inner leaflet to outer leaflet of lipid bilayer |
687517 |
| 7.6.2.2 | ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] |
the structure of Sav1866 reveals that tight interaction of the nucleotide-binding domains in the ATP-bound state is coupled to the outward-facing conformation of the transmembrane domains. In this conformation, bound substrates may escape into the outer leaflet of the lipid bilayer or into the aqueous medium surrounding the cell, depending on their hydrophobicity. Hydrolysis of ATP is expected to return the transporter to an inward-facing conformation, again granting access to the binding site from the cell interior. ABC transporters may thus use an alternating access and release mechanism first postulated for major facilitator transport proteins, with the distinction that ATP binding and hydrolysis, rather than substrate acquisition, may control the conversion of one state into the other |
-, 751692 |
| 7.6.2.2 | ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] |
thermodynamic data of ATP hydrolysis, mechanism |
659295 |
