EC Number   |
General Information |
Reference |
|---|
   7.6.2.2 | malfunction |
compared to the wild type strain, a deletion mutant of the enzyme is more vulnerable to detergents such as SDS and cholate, antibiotics such as tetracycline, oxytetracycline, chloramphenicol and minocycline, uncouplers including carbonyl cyanide 3-chlorophenylhydrazone and 2,4-dinitrophenol, membrane-permeable compounds such as tetraphenylphosphonium ion, heterocyclic dyes such as rhodamine 6G and acridine orange, DNA intercalating dyes such as ethidium bromide, and several other chemicals |
-, 733810 |
| 7.6.2.2 | malfunction |
enzyme deletion results in increased susceptibility to daunorubicin, doxorubicin, ethidium, and Hoechst 33342 |
-, 746765 |
| 7.6.2.2 | malfunction |
knockdown of enzyme expression reverses progesterone- and deoxycorticosterone-induced collateral sensitivity of CHO cells |
733268 |
| 7.6.2.2 | malfunction |
mutants lacking isoforms MDR3 and MDR5 have a reduced blood stage multiplication in vivo. Oocyst maturation and sporozoite formation in Plasmodium mutants lacking isoforms MDR2 or MDR5 is reduced |
748667 |
| 7.6.2.2 | malfunction |
rescue of the L1260A processing mutant by detergents, such as Triton X-100 or NP-35, but not of n-dodecyl-beta-D-maltoside. Only mutant I306C (TM5) shows highly activated ATPase activity (about 10fold greater than the untreated mutant) after treatment with MTS-verapamil while only mutant F343C shows highly activated ATPase activity (about 7fold higher than untreated) after treatment with MTS-rhodamine when labeling is performed in the presence or absence of n-dodecyl-beta-D-maltoside. All other mutants show less than a twofold activation after treatment in the presence or absence of detergent |
755956 |
| 7.6.2.2 | metabolism |
the enzyme is a lipophilic anion transporter that pumps endogenous and xenobiotic substrates from the cytoplasm to the extracellular milieu |
748832 |
| 7.6.2.2 | more |
the enzyme consists of 12 transmembrane helices in an arrangement that is consistent with cross-linking studies and electron microscopic imaging of the human multidrug resistance protein MDR1 (UniProt ID P08183), but critically different from that reported for the bacterial lipid flippase MsbA (UniProt ID P60752). The observed, outward-facing conformation reflects the ATP-bound state, with the two nucleotide-binding domains in close contact and the two transmembrane domains forming a central cavity, presumably the drug translocation pathway, that is shielded from the inner leaflet of the lipid bilayer and from the cytoplasm, but exposed to the outer leaflet and the extracellular space. Although ADP, rather than ATP, is bound, the nucleotide-binding domains in Sav1866 exhibit the conformation of the ATP-bound state. Substrate translocation pathway and structrue-function analysis, overview |
-, 751692 |
| 7.6.2.2 | physiological function |
absence of Mrp3 in knockout mice results in altered disposition of resveratrol-3-glucuronide and its parent compound resveratrol, leading to a reduced percentage of resveratrol being excreted via the urine in Mrp3-/- mice. Knockout of BCRP in mice results in high plasma levels of resveratrol-di-sulfate, a resveratrol metabolite hardly detectable in the plasma of wild-type mice and in an increased disposal of resveratrol via the urine |
700300 |
| 7.6.2.2 | physiological function |
human P-glycoprotein (P-gp, ABCB1) is a drug pump that catalyzes the ATP-dependent export of a wide variety of lipophilic compounds such as hydrophobic drugs, steroids, peptides, and detergents. Its physiological role is to protect the organism from cytotoxic compounds and plays an important role in the development of multidrug resistance |
755956 |
| 7.6.2.2 | physiological function |
mediates drug efflux from cells and plays a major role in causing multidrug resistance |
711926 |
