EC Number | Cloned (Comment) | Organism |
---|---|---|
7.6.2.2 | expression of wild-type and mutant enzymes in HEK-293 cell membranes | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
7.6.2.2 | P1150A | mutant MRP1 exhibits selectively increased estradiol glucuronide and methotrexate transport as well as altered interactions with ATP, the mutant displays very a low level of substrate-independent vanadate-induced trapping of [alphalpha32P]8N3ADP due to enhanced ADP release following ATP hydrolysis rather than a reduction in ATP hydrolysis itself. [alpha32P]8N3ADP trapping by MRP1-P1150A can be increased by using Ni2+ instead of Mg2+, and by decreasing temperature; however, the transport properties of the mutant remain unchanged | Homo sapiens |
7.6.2.2 | P1150G | mutant MRP1 exhibits selectively increased estradiol glucuronide and methotrexate transport as well as altered interactions with ATP, the mutant displays very a low level of substrate-independent vanadate-induced trapping of [alpha32P]8N3ADP due to enhanced ADP release following ATP hydrolysis rather than a reduction in ATP hydrolysis itself | Homo sapiens |
7.6.2.2 | P1150I | mutant MRP1 exhibits selectively increased estradiol glucuronide and methotrexate transport as well as altered interactions with ATP, the mutant displays very a low level of substrate-independent vanadate-induced trapping of [alpha32P]8N3ADP due to enhanced ADP release following ATP hydrolysis rather than a reduction in ATP hydrolysis itself | Homo sapiens |
7.6.2.2 | P1150L | mutant MRP1 exhibits selectively increased estradiol glucuronide and methotrexate transport as well as altered interactions with ATP, the mutant displays very a low level of substrate-independent vanadate-induced trapping of [alpha32P]8N3ADP due to enhanced ADP release following ATP hydrolysis rather than a reduction in ATP hydrolysis itself | Homo sapiens |
7.6.2.2 | P1150V | mutant MRP1 exhibits selectively increased estradiol glucuronide and methotrexate transport as well as altered interactions with ATP, the mutant displays very a low level of substrate-independent vanadate-induced trapping of [alpha32P]8N3ADP due to enhanced ADP release following ATP hydrolysis rather than a reduction in ATP hydrolysis itself | Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
7.6.2.2 | membrane | - |
Homo sapiens | 16020 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
7.6.2.2 | Mg2+ | - |
Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.6.2.2 | ATP + H2O + xenobiotic/in | Homo sapiens | the ATP-binding cassette multidrug resistance protein 1 mediates ATP-dependent cellular efflux of drugs and organic anions | ADP + phosphate + xenobiotic/out | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
7.6.2.2 | Homo sapiens | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
7.6.2.2 | recombinant wild-type and mutant enzymes from HEK-293 cells partially by membrane preparation | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.6.2.2 | ATP + H2O + xenobiotic/in | the ATP-binding cassette multidrug resistance protein 1 mediates ATP-dependent cellular efflux of drugs and organic anions | Homo sapiens | ADP + phosphate + xenobiotic/out | - |
? | |
7.6.2.2 | ATP + H2O + xenobiotic/in | functional importance of MRP1-Pro1150 at the interface of transmembrane helix 15 and cytoplasmic loop 7 | Homo sapiens | ADP + phosphate + xenobiotic/out | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
7.6.2.2 | MRP1 | - |
Homo sapiens |
7.6.2.2 | multidrug resistance protein 1 | - |
Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
7.6.2.2 | ATP | - |
Homo sapiens |