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Information on EC 7.6.2.2 - ABC-type xenobiotic transporter
for references in articles please use BRENDA:EC7.6.2.2
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EC Tree 7 Translocases
7.6 Catalysing the translocation of other compounds
7.6.2 Linked to the hydrolysis of a nucleoside triphosphate
7.6.2.2 ABC-type xenobiotic transporter
IUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. The enzymes from Gram-positive bacteria and eukaryotic cells 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 also transport glutathione—drug conjugates (see EC 7.6.2.3, ABC-type glutathione-S-conjugate transporter) while others also show some ’flippase’ activity (cf. EC 7.6.2.1, P-type phospholipid transporter).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 7.6.2.2
- verapamil
- doxorubicin
-
multidrug-resistant
-
blood-brain
- leukemia
-
cyclosporine
-
drug-resistant
- cholesterol
- xenobiotics
- rhodamine
-
disposition
- endothelial
- vincristine
-
caco-2
- paclitaxel
- cyp3a4
- vinblastine
-
chemosensitivity
- monolayers
-
chemoresistance
-
drug-drug
- cisplatin
- daunorubicin
- biliary
- etoposide
- adriamycin
-
pharmacodynamics
-
reversing
-
cross-resistance
-
basolateral
-
multi-drug
- anthracyclines
- digoxin
-
concentration-time
-
extrude
-
sublines
-
topoisomerase
- colchicine
-
pharmacogenetic
- docetaxel
- tacrolimus
- glucuronide
- hepatobiliary
- cyp2d6
-
pregnane
- cyp2c19
-
taxanes
- irinotecan
- ugt1a1
- ritonavir
- drug development
- diagnostics
- analysis
- pharmacology
- biofuel production
- medicine
Reaction Schemes
show+
+
xenobiotic[side 1]
=
+
+
xenobiotic[side 2]
Synonyms
p-glycoprotein, abcb1, abcg2, atp-binding cassette transporter, abcc2, breast cancer resistance protein, abcc1, multidrug resistance-associated protein, mdr1a, multidrug transporter, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ABC multidrug efflux transporter
ABC multidrug transporter
ABCB1
Abcb5
ABCC1
ABCC10
ABCC2
ABCC3
ABCC4
ABCG2
AcrB
acriflavine resistance protein
ATP phosphohydrolase (xenobiotic-exporting)
-
-
-
-
BCRP
BmrA
breast cancer resistance protein
canalicular multispecific organic anion transporter
Cdr1p
DrrAB
EC 3.6.3.44
-
-
formerly
-
EC 3.6.3.45
-
-
formerly
-
EfrAB
EfrCD
EfrEE
LmrA
MDR
MDR transporter
MDR1
Mdr1a
MDR1b
Mdr2
Mdr3
MDR4
MDR5
MDR6
MDR7
MdrP
MFS transporter
MRD1a
MRP
MRP1
MRP2
MRP3
MRP4
MRP5
MRP7
multidrug ABC transporter
multidrug resistance ABC transporter
multidrug resistance associated protein 5
multidrug resistance protein
multidrug resistance protein 1
multidrug resistance protein 2
multidrug resistance protein 3
multidrug resistance protein 4
multidrug resistance transporter
multidrug resistance transporter 1
multidrug resistance-associated protein 1
multidrug resistance-associated protein 2
multidrug transporter
multidrug-resistance protein
-
-
-
-
Na+(Li+, K+)/H+ antiporter
P-glycoprotein
P-gp
P-gp ABC transporter
Pdr18
PDR5
Pdr5p
Pgp
PGP1
Pgp2
Sav1866
Smr1
transporter protein MRP
-
-
-
-
xenobiotic-transporting ATPase
-
-
-
-
YdaG/YdbA
YvcC
additional information
ABCB1
-
-
ABCG2
-
breast cancer resistance protein
-
MDR1
-
-
MdrP
the enzyme exhibits dual functions as a Na+(Li+, K+)/H+ antiporter and a multidrug efflux pump
MdrP
Planococcus maritimus DS 17275T
the enzyme exhibits dual functions as a Na+(Li+, K+)/H+ antiporter and a multidrug efflux pump
-
MRP
-
-
-
-
MRP1
-
-
P-glycoprotein
-
-
-
-
P-glycoprotein
-
-
659188, 659295, 668705, 669989, 696343, 696714, 697006, 697110, 697586, 697712, 697766, 699450, 699463, 701069, 701435, 710872, 711073, 711157, 711411, 711833, 711893, 711894, 711926, 711931, 711970, 712696, 712710, 713201, 713202, 713592, 733332, 733539, 733820, 734280, 734441, 734442, 735307, 746663, 747041, 767685
P-gp
-
-
Pgp
-
-
-
-
additional information
-
Cdr1p is a multidrug transporter of the ATP-binding cassette superfamily
additional information
-
Cdr1p is a multidrug transporter of the ATP-binding cassette superfamily
-
additional information
-
ABCB1, or P-glycoprotein, is a member of the ATP binding cassette protein family
additional information
-
MRP4 is the shortest member of the MRP/ABCC C subfamily of ATP-binding cassette transporters
additional information
-
multidrug resistance proteins are members of the C branch of the ATP-binding cassette transporter superfamily
additional information
-
P-glycoprotein belongs to the family of ATP-binding cassette proteins
additional information
-
P-gp 170 is a member of the ATP-binding cassette, ABC, transporter superfamily
additional information
-
MRP4 is a member of the MRP/ABCC C subfamily of ATP-binding cassette transporters
additional information
-
Cdr1p is a multidrug transporter of the ATP-binding cassette superfamily
additional information
Nakaseomyces glabratus CCM8270
-
Cdr1p is a multidrug transporter of the ATP-binding cassette superfamily
-
additional information
-
P-glycoprotein is a member of the ATP-binding-cassette superfamily of proteins
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 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
-
ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2]
mechanism
-
ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2]
positive cooperativity mechanism
-
ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2]
mechanism
-
ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2]
thermodynamic data of ATP hydrolysis, mechanism
-
ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2]
thermodynamic data of ATP hydrolysis, mechanism
-
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
-
ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2]
P-gp mediated-transport mechanism, overview
-
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
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
-
-
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
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
oleandomycin activation/inactivation
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, xenobiotic-exporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. The enzymes from Gram-positive bacteria and eukaryotic cells 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 also transport glutathione---drug conjugates (see EC 7.6.2.3, ABC-type glutathione-S-conjugate transporter) while others also show some 'flippase' activity (cf. EC 7.6.2.1, P-type phospholipid transporter).
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-dinitrophenyl S-glutathione/in + ATP + H2O
2,4-dinitrophenyl S-glutathione/out + ADP + H2O
-
Substrates: -
Products: -
Products: -
?
3,6-bis(dimethylamino)-9-phenyl-selenoxanthylium bromide/in + ATP + H2O
3,6-bis(dimethylamino)-9-phenyl-selenoxanthylium bromide/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
3alpha-sulfatolithocholyltaurine/in + ATP + H2O
3alpha-sulfatolithocholyltaurine/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
6-mercaptopurine/in + ATP + H2O
6-mercaptopurine/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
8-aza-ATP + H2O + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/in
8-aza-ADP + phosphate + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/out
-
Substrates: 8-aza-ATP is a fairly good substrate of BmrA
Products: -
Products: -
?
8-azido-ATP + H2O + xenobiotic/in
8-azido-ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
9-(2-phosphonylmethoxyethyl)adenine/in + ATP + H2O
9-(2-phosphonylmethoxyethyl)adenine/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
aflatoxin B1-epoxide-GSH conjugate/in + ATP + H2O
aflatoxin B1-epoxide-GSH conjugate/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
aflatoxin B1/in + ATP + H2O
aflatoxin B1/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 1,13-bis[4'-(4H-chromen-4-on-2-yl)phenyl]-N-(benzyl)-1,4,10,13-tetraoxa-7-azatridecane/in
ADP + phosphate + 1,13-bis[4'-(4H-chromen-4-on-2-yl)phenyl]-N-(benzyl)-1,4,10,13-tetraoxa-7-azatridecane/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 17-beta-estradiol 17-(beta-D-glucuronide)[side 1]
ADP + phosphate + 17-beta-estradiol 17-(beta-D-glucuronide)[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + 17beta-estradiol 17-(beta-D-glucuronide)/in
ADP + phosphate + 17beta-estradiol 17-(beta-D-glucuronide)/out
ATP + H2O + 17beta-glucuronosyl oestradiol/in
ADP + phosphate + 17beta-glucuronosyl oestradiol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 2',3'-dideoxycytidine/in
ADP + phosphate + 2',3'-dideoxycytidine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein/in
ADP + phosphate + 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 2',7'-bis-(2-carboxyethyl)-5,6-carboxylfluoresceinacetoxymethyl ester/in
ADP + phosphate + 2',7'-bis-(2-carboxyethyl)-5,6-carboxylfluoresceinacetoxymethyl ester/out
ATP + H2O + 2',7'-bis-(3-carboxyethyl)-5-carboxyfluorescein/in
ADP + phosphate + 2',7'-bis-(3-carboxyethyl)-5-carboxyfluorescein/out
-
Substrates: fluorescent substrate
Products: -
Products: -
?
ATP + H2O + 2',7'-bis-(3-carboxyethyl)-6-carboxyfluorescein/in
ADP + phosphate + 2',7'-bis-(3-carboxyethyl)-6-carboxyfluorescein/out
-
Substrates: fluorescent substrate
Products: -
Products: -
?
ATP + H2O + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/in
ADP + phosphate + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/out
ATP + H2O + 2,3,5-triphenylterazolium chloride[side 1]
ADP + phosphate + 2,3,5-triphenylterazolium chloride[side 2]
ATP + H2O + 2,4-dinitrophenyl-S-glutathione[side 1]
ADP + phosphate + 2,4-dinitrophenyl-S-glutathione[side 2]
ATP + H2O + 2,5-dimethoxy-4-iodoamphetamine/in
ADP + phosphate + 2,5-dimethoxy-4-iodoamphetamine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 2,7'-bis-(carboxypropyl)-5(6)-carboxyfluorescein[side 1]
ADP + phosphate + 2,7'-bis-(carboxypropyl)-5(6)-carboxyfluorescein[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + 2,7-bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein acetoxymethyl ester[side 1]
ADP + phosphate + 2,7-bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein acetoxymethyl ester[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine[side 1]
ADP + phosphate + 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine[side 2]
ATP + H2O + 3,3'-dihexyloxacarbocyanine iodide/in
ADP + phosphate + 3,3'-dihexyloxacarbocyanine iodide/out
ATP + H2O + 3,4-methylenedioxy-alpha-ethylphenethylamine/in
ADP + phosphate + 3,4-methylenedioxy-alpha-ethylphenethylamine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 4-(2-aminoethyl)benzenesulfonylfluoride/in
ADP + phosphate + 4-(2-aminoethyl)benzenesulfonylfluoride/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 4-(methylnitrosoamino)-1-(3-pyridyl)-1-butanol[side 1]
ADP + phosphate + 4-(methylnitrosoamino)-1-(3-pyridyl)-1-butanol[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + 4-aminohippurate[side 1]
ADP + phosphate + 4-aminohippurate[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + 4-aminohippuric acid/in
ADP + phosphate + 4-aminohippuric acid/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 4-N-(2'-methoxystyryl)-thiosemicarbazone/in
ADP + phosphate + 4-N-(2'-methoxystyryl)-thiosemicarbazone/out
ATP + H2O + 4-nitroquinoline-1-oxide/in
ADP + phosphate + 4-nitroquinoline-1-oxide/out
-
Substrates: substrate for Snq2p
Products: -
Products: -
?
ATP + H2O + 5-(glutathione-S-yl)-N-methyl-alpha-methyldopamine/in
ADP + phosphate + 5-(glutathione-S-yl)-N-methyl-alpha-methyldopamine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 6-thioguanine[side 1]
ADP + phosphate + 6-thioguanine[side 2]
Substrates: substrate for ABCC4
Products: -
Products: -
?
ATP + H2O + 7-aminoactinomycin D/in
ADP + phosphate + 7-aminoactinomycin D/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + acitretin/in
ADP + phosphate + acitretin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + acridine orange[side 1]
ADP + phosphate + acridine orange[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + acriflavine [side 1]
ADP + phosphate + acriflavine[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + acriflavine[side 1]
ADP + phosphate + acriflavine[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + acriflavin[side 1]
ADP + phosphate + acriflavin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + actinomycin D/in
ADP + phosphate + actinomycin D/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + acyclovir/in
ADP + phosphate + acyclovir/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + adefovir/in
ADP + phosphate + adefovir/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + adevovir[side 1]
ADP + phosphate + adevovir[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + aflatoxin B[side 1]
ADP + phosphate + aflatoxin B[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + allopurinol/in
ADP + phosphate + allopurinol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + amprenavir[side 1]
ADP + phosphate + amprenavir[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + arsenite[side 1]
ADP + phosphate + arsenite[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + asimadoline[side 1]
ADP + phosphate + asimadoline[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + azacytidine[side 1]
ADP + phosphate + azacytidine[side 2]
Substrates: substrate for ABCC4
Products: -
Products: -
?
ATP + H2O + azidothymidine[side 1]
ADP + phosphate + azidothymidine[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + azole/in
ADP + phosphate + azole/out
-
Substrates: the ABC multidrug transporter Cdr1p plays a key role in azole resistance
Products: -
Products: -
?
ATP + H2O + bacitracin[side 1]
ADP + phosphate + bacitracin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + BCECF-acetoxymethylester[side 1]
ADP + phosphate + BCECF-acetoxymethylester[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + benzyltrimethylammonium[side 1]
ADP + phosphate + benzyltrimethylammonium[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + bepridil[side 1]
ADP + phosphate + bepridil[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + beta-estradiol 17-beta-D-glucuronide/in
ADP + phosphate + beta-estradiol 17-beta-D-glucuronide/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + beta-estradiol/in
ADP + phosphate + beta-estradiol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + bilirubin[side 1]
ADP + phosphate + bilirubin[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + bimatoprost/in
ADP + phosphate + bimatoprost/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + BODIPY-ethylenediamine[side 1]
ADP + phosphate + BODIPY-ethylenediamine[side 2]
-
Substrates: substrate of isoform Abcb4
Products: -
Products: -
?
ATP + H2O + BODIPY-prazosin[side 1]
ADP + phosphate + BODIPY-prazosin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Bodipy-verapamil/in
ADP + phosphate + Bodipy-verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + bodipy-vinblastine/in
ADP + phosphate + bodipy-vinblastine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + BODIPY-vinblastine[side 1]
ADP + phosphate + BODIPY-vinblastine[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + C12E08/in
ADP + phosphate + C12E08/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + caffeine/in
ADP + phosphate + caffeine/out
-
Substrates: Snq2p is a more functional transporter of caffeine than Pdr5p in yeast cells
Products: -
Products: -
?
ATP + H2O + calcein acetoxymethylester/in
ADP + phosphate + calcein acetoxymethylester/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + calcein acetoxymethylester[side 1]
ADP + phosphate + calcein acetoxymethylester[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + calcein AM[side 1]
ADP + phosphate + calcein AM[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + calcein-acetoxymethylester[side 1]
ADP + phosphate + calcein-acetoxymethylester[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + calphostin C[side 1]
ADP + phosphate + calphostin C[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + carboxydichlorofluorescein/in
ADP + phosphate + carboxydichlorofluorescein/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cefazolin/in
ADP + phosphate + cefazolin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cefmetazole/in
ADP + phosphate + cefmetazole/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cefodizime[side 1]
ADP + phosphate + cefodizime[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + cefoperazone[side 1]
ADP + phosphate + cefoperazone[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + cefotaxime/in
ADP + phosphate + cefotaxime/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + ceftizoxime/in
ADP + phosphate + ceftizoxime/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + celecoxib/in
ADP + phosphate + celecoxib/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cerivastatin[side 1]
ADP + phosphate + cerivastatin[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + chenodeoxycholic acid[side 1]
ADP + phosphate + chenodeoxycholic acid[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + chenodeoxycholylglycine/in
ADP + phosphate + chenodeoxycholylglycine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + chenodeoxycholyltaurine/in
ADP + phosphate + chenodeoxycholyltaurine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + chlorambucil[side 1]
ADP + phosphate + chlorambucil[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + chlorpromazine[side 1]
ADP + phosphate + chlorpromazine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + cholate/in
ADP + phosphate + cholate/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cholesterol[side 1]
ADP + phosphate + cholesterol[side 2]
Substrates: the enzyme does not catalyze significant cholesterol transport in vivo
Products: -
Products: -
?
ATP + H2O + cholic acid[side 1]
ADP + phosphate + cholic acid[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + cholylglycine/in
ADP + phosphate + cholylglycine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cholytaurine/in
ADP + phosphate + cholytaurine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + chrysin[side 1]
ADP + phosphate + chrysin[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + cidofovir[side 1]
ADP + phosphate + cidofovir[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + cisplatin[side 1]
ADP + phosphate + cisplatin[side 2]
Substrates: substrate for P-glycoprotein and MPR2
Products: -
Products: -
?
ATP + H2O + clorambucil[side 1]
ADP + phosphate + clorambucil[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + corticosterone/in
ADP + phosphate + corticosterone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + coumermycin A1[side 1]
ADP + phosphate + coumermycin A1[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cyclic guanosine monophosphate/in
ADP + phosphate + cyclic guanosine monophosphate/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cycloheximide /in
ADP + phosphate + cycloheximide /out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cyclophosphamide[side 1]
ADP + phosphate + cyclophosphamide[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + cyclosporin A[side 1]
ADP + phosphate + cyclosporin A[side 2]
Substrates: substrate for P-glycoprotein and BCRP
Products: -
Products: -
?
ATP + H2O + cyclosporin H[side 1]
ADP + phosphate + cyclosporin H[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + cyclosporine A/in
ADP + phosphate + cyclosporine A/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cyclosporine A[side 1]
ADP + phosphate + cyclosporine A [side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + cyclosporine[side 1]
ADP + phosphate + cyclosporine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + cytarabine/in
ADP + phosphate + cytarabine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + darunavir/in
ADP + phosphate + darunavir/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunomycin[side 1]
ADP + phosphate + daunomycin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + dehydroepiandrosterone sulfate/in
ADP + phosphate + dehydroepiandrosterone sulfate/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + dehydroepiandrosterone sulfate[side 1]
ADP + phosphate + dehydroepiandrosterone sulfate[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + dehydroepiandrosterone-3-sulfate/in
ADP + phosphate + dehydroepiandrosterone-3-sulfate/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + delavirdine[side 1]
ADP + phosphate + delavirdine[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + deoxycholic acid[side 1]
ADP + phosphate + deoxycholic acid[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + deoxycholylglycine/in
ADP + phosphate + deoxycholylglycine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + deoxycorticosterone/in
ADP + phosphate + deoxycorticosterone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + dexamethasone/in
ADP + phosphate + dexamethasone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + diclofenac/in
ADP + phosphate + diclofenac/out
-
Substrates: substrate of BCRP, but not of P-gp and MDR1
Products: -
Products: -
?
ATP + H2O + digitonin[side 1]
ADP + phosphate + digitonin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + digoxin/in
ADP + phosphate + digoxin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + digoxin[side 1]
ADP + phosphate + digoxin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + diltiazem[side 1]
ADP + phosphate + diltiazem[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + dimethylarsenic acid[side 1]
ADP + phosphate + dimethylarsenic acid[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + dinitrophenyl[side 1]
ADP + phosphate + dinitrophenyl[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + dipyridamole/in
ADP + phosphate + dipyridamole/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + dipyridamole[side 1]
ADP + phosphate + dipyridamole[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + docetaxel/in
ADP + phosphate + docetaxel/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + docetaxel[side 1]
ADP + phosphate + docetaxel[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + dodecyloctaglycol/in
ADP + phosphate + dodecyloctaglycol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxycycline[side 1]
ADP + phosphate + doxycycline[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + E217betaG/in
ADP + phosphate + E217betaG/out
-
Substrates: MRP3 preferentially transports E217betaG with a medium affinity and a very high capacity, while MRP1 transports E217betaG with a higher affinity but with much lower capacity
Products: -
Products: -
?
ATP + H2O + echonocandin B[side 1]
ADP + phosphate + echonocandin B[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + edaravone glucuronide/in
ADP + phosphate + edaravone glucuronide/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + endosulfan[side 1]
ADP + phosphate + endosulfan[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + epirubicin[side 1]
ADP + phosphate + epirubicin[side 2]
Substrates: substrate for P-glycoprotein, BCRP, and MPR2
Products: -
Products: -
?
ATP + H2O + epothilone B/in
ADP + phosphate + epothilone B/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + estradiol 17-beta-D-glucuronide/in
ADP + phosphate + estradiol 17-beta-D-glucuronide/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + estradiol 17-beta-glucuronide[side 1]
ADP + phosphate + estradiol 17-beta-glucuronide[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + estradiol glucuronide/in
ADP + phosphate + estradiol glucuronide/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + estradiol[side 1]
ADP + phosphate + estradiol[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + estrone 3-sulfate[side 1]
ADP + phosphate + estrone 3-sulfate[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + estrone[side 1]
ADP + phosphate + estrone[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + ethacrynic acid[side 1]
ADP + phosphate + ethacrynic acid[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + ethinylestradiol-3-O-glucuronide[side 1]
ADP + phosphate + ethinylestradiol-3-O-glucuronide[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + felodipine[side 1]
ADP + phosphate + felodipine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + fenbuconazole/in
ADP + phosphate + fenbuconazole/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + fentanyl[side 1]
ADP + phosphate + fentanyl[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + fexofenadine/in
ADP + phosphate + fexofenadine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + fexofenadine[side 1]
ADP + phosphate + fexofenadine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + FK-506[side 1]
ADP + phosphate + FK-506[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + FK506[side 1]
ADP + phosphate + FK506[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + fluoroquinolone/in
ADP + phosphate + fluoroquinolone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Flutax[side 1]
ADP + phosphate + Flutax[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + folic acid/in
ADP + phosphate + folic acid/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + folic acid[side 1]
ADP + phosphate + folic acid[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + gemcitabine/in
ADP + phosphate + gemcitabine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + genistein-7-glucoside[side 1]
ADP + phosphate + genistein-7-glucoside[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + gentamycin[side 1]
ADP + phosphate + gentamycin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + glaucine/in
ADP + phosphate + glaucine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + glutathione disulfide[side 1]
ADP + phosphate + glutathione disulfide[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + glutathione/in
ADP + phosphate + glutathione/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + glycocholic acid[side 1]
ADP + phosphate + glycocholic acid[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + gramicidin A[side 1]
ADP + phosphate + gramicidin A[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + gramicidin D[side 1]
ADP + phosphate + gramicidin D[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + grepafloxacine[side 1]
ADP + phosphate + grepafloxacine[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + grepafloxacin[side 1]
ADP + phosphate + grepafloxacin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + GSH-conjugated 4-hydroxy-2-nonenal/in
ADP + phosphate + GSH-conjugated 4-hydroxy-2-nonenal/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + GSH-conjugated prostaglandin A2/in
ADP + phosphate + GSH-conjugated prostaglandin A2/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + GSSG/in
ADP + phosphate + GSSG/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + guanidinium ion[side 1]
ADP + phosphate + guanidinium ion[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + H33342/in
ADP + phosphate + H33342/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + harmane[side 1]
ADP + phosphate + harmane[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + hematoporphyrin[side 1]
ADP + phosphate + hematoporphyrin[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + hydrochlorothiazide/in
ADP + phosphate + hydrochlorothiazide/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + hydroxyurea[side 1]
ADP + phosphate + hydroxyurea[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + imatinib[side 1]
ADP + phosphate + imatinib[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + irinotecan[side 1]
ADP + phosphate + irinotecan[side 2]
Substrates: substrate for P-glycoprotein, BCRP, and MPR2
Products: -
Products: -
?
ATP + H2O + itraconazole/in
ADP + phosphate + itraconazole/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + itraconazole[side 1]
ADP + phosphate + itraconazole[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + kanamicin[side 1]
ADP + phosphate + kanamicin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + lamivudine[side 1]
ADP + phosphate + lamivudine[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + latanoprost/in
ADP + phosphate + latanoprost/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + LDS 751[side 1]
ADP + phosphate + LDS 751[side 2]
-
Substrates: substrate of isoform Abcb4
Products: -
Products: -
?
ATP + H2O + leucovorin/in
ADP + phosphate + leucovorin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + leucovorin[side 1]
ADP + phosphate + leucovorin[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + leukotriene B4/in
ADP + phosphate + leukotriene B4/out
-
Substrates: MRP4 only transports leukotriene B4 in the presence of glutathione
Products: -
Products: -
?
ATP + H2O + leukotriene D4[side 1]
ADP + phosphate + leukotriene D4[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + leukotriene E4/in
ADP + phosphate + leukotriene E4/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + leupeptin[side 1]
ADP + phosphate + leupeptin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + levofloxacin[side 1]
ADP + phosphate + levofloxacin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + lidocaine[side 1]
ADP + phosphate + lidocaine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + lithocholic acid[side 1]
ADP + phosphate + lithocholic acid[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + loratadine/in
ADP + phosphate + loratadine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + lovastatin[side 1]
ADP + phosphate + lovastatin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + lyso-tracker green[side 1]
ADP + phosphate + lyso-tracker green[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + lysophosphatidylinositol/in
ADP + phosphate + lysophosphatidylinositol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + malachite green/in
ADP + phosphate + malachite green/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + melphalan[side 1]
ADP + phosphate + melphalan[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + methyl parathion[side 1]
ADP + phosphate + methyl parathion[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + methyltriphenylphosphonium[side 1]
ADP + phosphate + methyltriphenylphosphonium[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + minocycline[side 1]
ADP + phosphate + minocycline[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + misoprostol/in
ADP + phosphate + misoprostol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + mitoxantrone/in
ADP + phosphate + mitoxantrone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + monensin/in
ADP + phosphate + monensin/out
-
Substrates: affinity of verapamil to MDR1 is not affected by pH value. Protein concentration is inversely related to the maximum activation of ATPase activity achieved
Products: -
Products: -
?
ATP + H2O + monoglucuronosyl bilirubin/in
ADP + phosphate + monoglucuronosyl bilirubin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + morphine[side 1]
ADP + phosphate + morphine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + MTS-rhodamine [side 1]
ADP + phosphate + MTS-rhodamine [side 2]
Substrates: the binding site in transmembrane segment 5 is F343C for rhodamine
Products: -
Products: -
?
ATP + H2O + N-(1-phenylcyclohexyl)-3-ethoxypropanamine/in
ADP + phosphate + N-(1-phenylcyclohexyl)-3-ethoxypropanamine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + N-(2'-deoxy-beta-D-ribofuranosyl)-5-cyclohexyl-1H-indole/in
?
-
Substrates: nontransported substrate of P-glycoprotein
Products: -
Products: -
?
ATP + H2O + N-benzyl-2-nitro-1H-imidazole-1-acetamide/in
ADP + phosphate + N-benzyl-2-nitro-1H-imidazole-1-acetamide/out
ATP + H2O + n-dodecyl-N,N-dimethylamine N-oxide[side 1]
ADP + phosphate + n-dodecyl-N,N-dimethylamine N-oxide[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + N-ethylmaleimide S-glutathione/in
ADP + phosphate + N-ethylmaleimide S-glutathione/out
ATP + H2O + N-isopropyl-1,2-diphenylethylamine/in
ADP + phosphate + N-isopropyl-1,2-diphenylethylamine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + nicardipine/in
ADP + phosphate + nicardipine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + nifedipine/in
ADP + phosphate + nifedipine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + nifedipine[side 1]
ADP + phosphate + nifedipine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + nisoldipine[side 1]
ADP + phosphate + nisoldipine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + nitrendipine[side 1]
ADP + phosphate + nitrendipine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + novobiocin[side 1]
ADP + phosphate + novobiocin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + oligomycin/in
ADP + phosphate + oligomycin/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + olmesartan/in
ADP + phosphate + olmesartan/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + olmesartan[side 1]
ADP + phosphate + olmesartan[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + ortataxel[side 1]
ADP + phosphate + ortataxel[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + p-methoxy-ethylamphetamine/in
ADP + phosphate + p-methoxy-ethylamphetamine/out
ATP + H2O + para-methoxy-ethylamphetamine/in
ADP + phosphate + para-methoxy-ethylamphetamine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + paraquat[side 1]
ADP + phosphate + paraquat[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + pentazocine[side 1]
ADP + phosphate + pentazocine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + pepstatin A[side 1]
ADP + phosphate + pepstatin A[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + phenothiazine[side 1]
ADP + phosphate + phenothiazine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + phenylguanidinium[side 1]
ADP + phosphate + phenylguanidinium[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + pheophorbide A[side 1]
ADP + phosphate + pheophorbide A[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + phloridzin[side 1]
ADP + phosphate + phloridzin[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + phosphatidylcholine/in
ADP + phosphate + phosphatidylcholine/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + pirarubicin/in
ADP + phosphate + pirarubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + pravastatin[side 1]
ADP + phosphate + pravastatin[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + prazosin[side 1]
ADP + phosphate + prazosin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + progesterone[side 1]
ADP + phosphate + progesterone[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + propafenone[side 1]
ADP + phosphate + propafenone[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + propidium[side 1]
ADP + phosphate + propidium[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + prostaglandin A2/in
ADP + phosphate + prostaglandin A2/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + prostaglandin E1/in
ADP + phosphate + prostaglandin E1/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + prostaglandin E2/in
ADP + phosphate + prostaglandin E2/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + prostaglandin E2[side 1]
ADP + phosphate + prostaglandin E2[side 2]
Substrates: substrate for MRP1
Products: -
Products: -
?
ATP + H2O + prostaglandin F2alpha/in
ADP + phosphate + prostaglandin F2alpha/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + PSC-833[side 1]
ADP + phosphate + PSC-833[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + puromycin/in
ADP + phosphate + puromycin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + quercetin 4'-beta-glucoside[side 1]
ADP + phosphate + quercetin 4'-beta-glucoside[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + ranitidine[side 1]
ADP + phosphate + ranitidine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + rapamycin[side 1]
ADP + phosphate + rapamycin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + repaglinide/in
ADP + phosphate + repaglinide/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + reserpine[side 1]
ADP + phosphate + reserpine[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + resveratrol disulfate/in
ADP + phosphate + resveratrol disulfate/out
-
Substrates: substrate of BCRP in vitro
Products: -
Products: -
?
ATP + H2O + resveratrol-3-glucuronide/in
ADP + phosphate + resveratrol-3-glucuronide/out
-
Substrates: substrate of Mrp3 and BCRP in vitro as sulfate
Products: -
Products: -
?
ATP + H2O + resveratrol-3-sulfate [side 1]
ADP + phosphate + resveratrol-3-sulfate [side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + resveratrol/in
ADP + phosphate + resveratrol/out
-
Substrates: substrate of BCRP in vitro as sulfate
Products: -
Products: -
?
ATP + H2O + rhodamine 123 /in
ADP + phosphate + rhodamine 123 /out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 6-G/in
ADP + phosphate + rhodamine 6-G/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine B/in
ADP + phosphate + rhodamine B/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine-123[side 1]
ADP + phosphate + rhodamine-123[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rifampicin/in
ADP + phosphate + rifampicin/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + rifampin[side 1]
ADP + phosphate + rifampin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rosuvastatin[side 1]
ADP + phosphate + rosuvastatin[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + roxithromycin[side 1]
ADP + phosphate + roxithromycin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + S-2,4-dinitrophenylglutathione/in
ADP + phosphate + S-2,4-dinitrophenylglutathione/out
ATP + H2O + salmeterol/in
ADP + phosphate + salmeterol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + saquinavir/in
ADP + phosphate + saquinavir/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + simvastatin[side 1]
ADP + phosphate + simvastatin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + sirolimus[side 1]
ADP + phosphate + sirolimus[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + sodium cholate[side 1]
ADP + phosphate + sodium cholate[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + sorafenib[side 1]
ADP + phosphate + sorafenib[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + sparfloxacin[side 1]
ADP + phosphate + sparfloxacin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + spectinomycin[side 1]
ADP + phosphate + spectinomycin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + sphingosine-1-phosphate/in
ADP + phosphate + sphingosine-1-phosphate/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + staurosporine[side 1]
ADP + phosphate + staurosporine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + tacrolimus[side 1]
ADP + phosphate + tacrolimus[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + talinolol/in
ADP + phosphate + talinolol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + tariquidar [side 1]
ADP + phosphate + tariquidar [side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + taurochenodeoxycholic acid[side 1]
ADP + phosphate + taurochenodeoxycholic acid[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + taurocholate/in
ADP + phosphate + taurocholate/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + taurodeoxycholic acid[side 1]
ADP + phosphate + taurodeoxycholic acid[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + taurolithocholic acid[side 1]
ADP + phosphate + taurolithocholic acid[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + telmisartan/in
ADP + phosphate + telmisartan/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + temocaprilate[side 1]
ADP + phosphate + temocaprilate[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + temozolomide[side 1]
ADP + phosphate + temozolomide[side 2]
Substrates: substrate for ABCB1
Products: -
Products: -
?
ATP + H2O + tenofovir/in
ADP + phosphate + tenofovir/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + terfenadine[side 1]
ADP + phosphate + terfenadine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + tetramethylrhodamine ethyl ester[side 1]
ADP + phosphate + tetramethylrhodamine ethyl ester[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + tetramethylrhodamine/in
ADP + phosphate + tetramethylrhodamine/out
-
Substrates: better substrate than rhodamine 123, temperature dependence of the rate of tetramethylrosamine transport, the rate of drug transport may be dominated by partitioning of drug into the membrane bilayer
Products: -
Products: -
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ATP + H2O + tetraphenylphosphonium[side 1]
ADP + phosphate + tetraphenylphosphonium[side 2]
ATP + H2O + tetrapropylammonium[side 1]
ADP + phosphate + tetrapropylammonium[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + thromboxane B2/in
ADP + phosphate + thromboxane B2/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + tiapamil[side 1]
ADP + phosphate + tiapamil[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + topotecan/in
ADP + phosphate + topotecan/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + trans-flupentixol[side 1]
ADP + phosphate + trans-flupentixol[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + trifluoperazine[side 1]
ADP + phosphate + trifluoperazine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + ursodeoxycholylglycine/in
ADP + phosphate + ursodeoxycholylglycine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + ursodeoxycholyltaurine/in
ADP + phosphate + ursodeoxycholyltaurine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + valinomycin[side 1]
ADP + phosphate + valinomycin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + valspodar[side 1]
ADP + phosphate + valspodar[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + verapamil [side 1]
ADP + phosphate + verapamil [side 2]
Substrates: the binding site in transmembrane segment 5 is I306C for verapamil
Products: -
Products: -
?
ATP + H2O + vinblastine sulfate/in
ADP + phosphate + vinblastine sulfate/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + vincristine sulfate/in
ADP + phosphate + vincristine sulfate/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + vincristine/in
ADP + phosphate + vincristine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + zidovudine[side 1]
ADP + phosphate + zidovudine[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + [1,2,6,7-3H(N)]dehydroepiandrosterone-3-sulfate/in
ADP + phosphate + [1,2,6,7-3H(N)]dehydroepiandrosterone-3-sulfate/out
-
Substrates: -
Products: -
Products: -
?
bacitracin/in + ATP + H2O
bacitracin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
chloramphenicol/in + ATP + H2O
chloramphenicol/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
clotrimazole/in + ATP + H2O
clotrimazole/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
colchicine/in + ATP + H2O
colchicine/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
CTP + H2O + ketoconazole[side 1]
CDP + phosphate + ketoconazole[side 2]
-
Substrates: -
Products: -
Products: -
?
CTP + H2O + rhodamine 6 G[side 1]
CDP + phosphate + rhodamine 6 G[side 2]
-
Substrates: -
Products: -
Products: -
?
CTP + H2O + rhodamine 6G/in
CDP + phosphate + rhodamine 6G/out
-
Substrates: low CTPase activity
Products: -
Products: -
?
cyclo(D-Trp-D-Asp-L-Pro-D-Val-L-Leu)/in + ATP + H2O
cyclo(D-Trp-D-Asp-L-Pro-D-Val-L-Leu)/out + ADP + phosphate
cysteinyl leukotriene C4/in + ATP + H2O
cysteinyl leukotriene C4/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
daunomycin/in + ATP + H2O
daunomycin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
dexamethasone/in + ATP + H2O
dexamethasone/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
digoxin/in + ATP + H2O
digoxin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
estradiol 17-beta-D-glucuronide/in + ATP + H2O
estradiol 17-beta-D-glucuronide/out + ADP + phosphate
ethidium bromide/in + ATP + H2O
ethidium bromide/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
glycocholate/in + ATP + H2O
glycocholate/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
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GTP + H2O + ciprofloxacin[side 1]
GDP + phosphate + ciprofloxacin[side 2]
-
Substrates: the enzyme has much higher GTPase activity as compared to its ATPase activity
Products: -
Products: -
?
GTP + H2O + coumermycin A1[side 1]
GDP + phosphate + coumermycin A1[side 2]
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + doxorubicin/in
GDP + phosphate + doxorubicin/out
Substrates: highest efficiency
Products: -
Products: -
?
GTP + H2O + doxorubicin[side 1]
GDP + phosphate + doxorubicin[side 2]
-
Substrates: the enzyme has much higher GTPase activity as compared to its ATPase activity
Products: -
Products: -
?
GTP + H2O + ethidium[side 1]
GDP + phosphate + ethidium[side 2]
-
Substrates: -
Products: -
Products: -
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GTP + H2O + Hoechst33342[side 1]
GDP + phosphate + Hoechst33342[side 2]
-
Substrates: the enzyme has much higher GTPase activity as compared to its ATPase activity. Hoechst 33342 is 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole
Products: -
Products: -
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GTP + H2O + ketoconazole[side 1]
GDP + phosphate + ketoconazole[side 2]
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + norfloxacin[side 1]
GDP + phosphate + norfloxacin[side 2]
-
Substrates: the enzyme has much higher GTPase activity as compared to its ATPase activity
Products: -
Products: -
?
GTP + H2O + novobiocin[side 1]
GDP + phosphate + novobiocin[side 2]
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + propidium[side 1]
GDP + phosphate + propidium[side 2]
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + rhodamine 6 G[side 1]
GDP + phosphate + rhodamine 6 G[side 2]
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + rhodamine 6G/in
GDP + phosphate + rhodamine 6G/out
-
Substrates: -
Products: -
Products: -
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Hoechst 33342/in + ATP + H2O
Hoechst 33342/out + ADP + H2O
-
Substrates: i.e. 2-[2-(4-ethoxyphenyl)-6-benzimidazolyl]-6-(1-methyl-4-piperazinyl)benzimidazole
Products: -
Products: -
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leukotriene E4/in + ATP + H2O
leukotriene E4/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
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methotrexate/in + ATP + H2O
methotrexate/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate/in + ATP + H2O
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]thiochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
nicardipine/in + ATP + H2O
nicardipine/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
novobiocin/in + ATP + H2O
novobiocin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
paclitaxel/in + ATP + H2O
paclitaxel/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
pentachlorophenol/in + ATP + H2O
pentachlorophenol/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
phenol/in + ATP + H2O
phenol/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
rhodamine B/in + ATP + H2O
rhodamine B/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
S-(2,4-dinitrophenyl)glutathione/in + ATP + H2O
S-(2,4-dinitrophenyl)glutathione/out + ADP + phosphate
streptomycin/in + ATP + H2O
streptomycin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
streptothricin/in + ATP + H2O
streptothricin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
taxol/in + ATP + H2O
taxol/out + ADP + H2O
-
Substrates: weak activity
Products: -
Products: -
?
tetrachlorohydroquinone/in + ATP + H2O
tetrachlorohydroquinone/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
tobramycin/in + ATP + H2O
tobramycin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
UTP + H2O + rhodamine 6G/in
UDP + phosphate + rhodamine 6G/out
-
Substrates: low UTPase activity
Products: -
Products: -
?
valinomycin/in + ATP + H2O
valinomycin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
verapamil/in + ATP + H2O
verapamil/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: ATP binding to Cdr1p is not a prerequisite for drug binding and both drug as well as ATP binding, which induce specific conformational changes, can occur independently of each other
Products: -
Products: -
?
ATP + H2O + 17beta-estradiol 17-(beta-D-glucuronide)/in
ADP + phosphate + 17beta-estradiol 17-(beta-D-glucuronide)/out
-
Substrates: transported by MRP1 and MRP3
Products: -
Products: -
?
ATP + H2O + 17beta-estradiol 17-(beta-D-glucuronide)/in
ADP + phosphate + 17beta-estradiol 17-(beta-D-glucuronide)/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 17beta-estradiol 17-(beta-D-glucuronide)/in
ADP + phosphate + 17beta-estradiol 17-(beta-D-glucuronide)/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 2',7'-bis-(2-carboxyethyl)-5,6-carboxylfluoresceinacetoxymethyl ester/in
ADP + phosphate + 2',7'-bis-(2-carboxyethyl)-5,6-carboxylfluoresceinacetoxymethyl ester/out
Substrates: YdaG/YdbA heterodimer
Products: -
Products: -
?
ATP + H2O + 2',7'-bis-(2-carboxyethyl)-5,6-carboxylfluoresceinacetoxymethyl ester/in
ADP + phosphate + 2',7'-bis-(2-carboxyethyl)-5,6-carboxylfluoresceinacetoxymethyl ester/out
Substrates: YdaG/YdbA heterodimer
Products: -
Products: -
?
ATP + H2O + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/in
ADP + phosphate + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/out
-
Substrates: Hoechst 33342, ABC transporter YvcC
Products: -
Products: -
?
ATP + H2O + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/in
ADP + phosphate + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/out
-
Substrates: Hoechst 33342, half-ABC transporter BmrA, Glu-504, adjacent to the Walker-B motif, is the catalytic base for ATP hydrolysis
Products: -
Products: -
?
ATP + H2O + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/in
ADP + phosphate + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/out
-
Substrates: Hoechst 33342
Products: -
Products: -
?
ATP + H2O + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/in
ADP + phosphate + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/out
-
Substrates: Hoechst 33342 binding site, proximity of bound Hoechst 33342 to the ATPase catalytic sites places the drug binding site of P-glycoprotein within the cytoplasmic membrane leaflet, Cys-428 and Cys-1071 are within the catalytic sites of Pgp, one within each of the Walker A motifs of the nucleotide binding folds, mechanism
Products: -
Products: -
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ATP + H2O + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/in
ADP + phosphate + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/out
-
Substrates: Hoechst 33342
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Products: -
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ATP + H2O + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/in
ADP + phosphate + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/out
-
Substrates: Hoechst 33342
Products: -
Products: -
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ATP + H2O + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/in
ADP + phosphate + 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bis-1H-benzimidazole/out
Substrates: Hoechst 33342, YdaG/YdbA heterodimer
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ATP + H2O + 2,3,5-triphenylterazolium chloride[side 1]
ADP + phosphate + 2,3,5-triphenylterazolium chloride[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + 2,3,5-triphenylterazolium chloride[side 1]
ADP + phosphate + 2,3,5-triphenylterazolium chloride[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 2,4-dinitrophenyl-S-glutathione[side 1]
ADP + phosphate + 2,4-dinitrophenyl-S-glutathione[side 2]
Substrates: -
Products: -
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?
ATP + H2O + 2,4-dinitrophenyl-S-glutathione[side 1]
ADP + phosphate + 2,4-dinitrophenyl-S-glutathione[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine[side 1]
ADP + phosphate + 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine[side 2]
Substrates: -
Products: -
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ATP + H2O + 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine[side 1]
ADP + phosphate + 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine[side 2]
Substrates: -
Products: -
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ATP + H2O + 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine[side 1]
ADP + phosphate + 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + 3,3'-dihexyloxacarbocyanine iodide/in
ADP + phosphate + 3,3'-dihexyloxacarbocyanine iodide/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + 3,3'-dihexyloxacarbocyanine iodide/in
ADP + phosphate + 3,3'-dihexyloxacarbocyanine iodide/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + 4-N-(2'-methoxystyryl)-thiosemicarbazone/in
ADP + phosphate + 4-N-(2'-methoxystyryl)-thiosemicarbazone/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + 4-N-(2'-methoxystyryl)-thiosemicarbazone/in
ADP + phosphate + 4-N-(2'-methoxystyryl)-thiosemicarbazone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 5-fluorouracil[side 1]
ADP + phosphate + 5-fluorouracil[side 2]
Substrates: substrate for ABCB1
Products: -
Products: -
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ATP + H2O + 5-fluorouracil[side 1]
ADP + phosphate + 5-fluorouracil[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + 9-hydroxyrisperidone/in
ADP + phosphate + 9-hydroxyrisperidone/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + 9-hydroxyrisperidone/in
ADP + phosphate + 9-hydroxyrisperidone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + actinomycin D[side 1]
ADP + phosphate + actinomycin D[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + actinomycin D[side 1]
ADP + phosphate + actinomycin D[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + actinomycin D[side 1]
ADP + phosphate + actinomycin D[side 2]
Substrates: substrate for ABCB1
Products: -
Products: -
?
ATP + H2O + actinomycin D[side 1]
ADP + phosphate + actinomycin D[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
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ATP + H2O + amiodarone[side 1]
ADP + phosphate + amiodarone[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
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ATP + H2O + amiodarone[side 1]
ADP + phosphate + amiodarone[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
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ATP + H2O + ampicillin[side 1]
ADP + phosphate + ampicillin[side 2]
Substrates: -
Products: -
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ATP + H2O + ampicillin[side 1]
ADP + phosphate + ampicillin[side 2]
Substrates: substrate for MPR2
Products: -
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?
ATP + H2O + anisomycin/in
ADP + phosphate + anisomycin/out
-
Substrates: recombinant Cdr1p
Products: -
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ATP + H2O + anisomycin/in
ADP + phosphate + anisomycin/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + azidopine[side 1]
ADP + phosphate + azidopine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + azidopine[side 1]
ADP + phosphate + azidopine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
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ATP + H2O + azithromycin[side 1]
ADP + phosphate + azithromycin[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
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ATP + H2O + azithromycin[side 1]
ADP + phosphate + azithromycin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + azithromycin[side 1]
ADP + phosphate + azithromycin[side 2]
Planococcus maritimus DS 17275T
Substrates: -
Products: -
Products: -
?
ATP + H2O + bisantrene[side 1]
ADP + phosphate + bisantrene[side 2]
-
Substrates: poor transport by isoform Abcb5 compared to Abcb4
Products: -
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ATP + H2O + bisantrene[side 1]
ADP + phosphate + bisantrene[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + buspirone/in
ADP + phosphate + buspirone/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + buspirone/in
ADP + phosphate + buspirone/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + calcein/in
ADP + phosphate + calcein/out
-
Substrates: -
Products: -
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ATP + H2O + calcein/in
ADP + phosphate + calcein/out
-
Substrates: fluorescent substrate of MRP1
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ATP + H2O + calcein/in
ADP + phosphate + calcein/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + calcein[side 1]
ADP + phosphate + calcein[side 2]
Substrates: substrate for MRP1
Products: -
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ATP + H2O + calcein[side 1]
ADP + phosphate + calcein[side 2]
-
Substrates: -
Products: -
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ATP + H2O + calcein[side 1]
ADP + phosphate + calcein[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + ceftriaxone[side 1]
ADP + phosphate + ceftriaxone[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
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ATP + H2O + ceftriaxone[side 1]
ADP + phosphate + ceftriaxone[side 2]
Substrates: substrate for MPR2
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Products: -
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ATP + H2O + chloramphenicol[side 1]
ADP + phosphate + chloramphenicol[side 2]
Substrates: -
Products: -
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ATP + H2O + chloramphenicol[side 1]
ADP + phosphate + chloramphenicol[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + chlorpromazine/in
ADP + phosphate + chlorpromazine/out
-
Substrates: -
Products: -
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ATP + H2O + chlorpromazine/in
ADP + phosphate + chlorpromazine/out
-
Substrates: -
Products: -
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ATP + H2O + cholesterol/in
ADP + phosphate + cholesterol/out
-
Substrates: P-gp may actively mediate cholesterol redistribution in the cell membrane, P-gp mediates the ATP-dependent relocation of cholesterol from the cytosolic leaflet to the exoplasmic leaflet of the plasma membrane, P-gp likely contributes in stabilizing the cholesterol-rich microdomains, rafts and caveolae, and is involved in the regulation of cholesterol trafficking in cells
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ATP + H2O + cholesterol/in
ADP + phosphate + cholesterol/out
-
Substrates: P-gp may actively mediate cholesterol redistribution in the cell membrane, in the absence of substrates P-gp exhibits an apparently futile, basal ATPase activity, which is tightly dependent on the presence of cholesterol in the membrane by using native membrane vesicles containing high amounts of P-gp
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ATP + H2O + cimetidine[side 1]
ADP + phosphate + cimetidine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + cimetidine[side 1]
ADP + phosphate + cimetidine[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + ciprofloxacin[side 1]
ADP + phosphate + ciprofloxacin[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + ciprofloxacin[side 1]
ADP + phosphate + ciprofloxacin[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + ciprofloxacin[side 1]
ADP + phosphate + ciprofloxacin[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + ciprofloxacin[side 1]
ADP + phosphate + ciprofloxacin[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + citalopram/in
ADP + phosphate + citalopram/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + citalopram/in
ADP + phosphate + citalopram/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + clarithromycin[side 1]
ADP + phosphate + clarithromycin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + clarithromycin[side 1]
ADP + phosphate + clarithromycin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + clarithromycin[side 1]
ADP + phosphate + clarithromycin[side 2]
Planococcus maritimus DS 17275T
Substrates: -
Products: -
Products: -
?
ATP + H2O + clotrimazole/in
ADP + phosphate + clotrimazole/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + clotrimazole/in
ADP + phosphate + clotrimazole/out
-
Substrates: substrate for Pdr5p
Products: -
Products: -
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ATP + H2O + colchicine/in
ADP + phosphate + colchicine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + colchicine/in
ADP + phosphate + colchicine/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + colchicine[side 1]
ADP + phosphate + colchicine[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + colchicine[side 1]
ADP + phosphate + colchicine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + colchicine[side 1]
ADP + phosphate + colchicine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + colchicine[side 1]
ADP + phosphate + colchicine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + cyclobenzaprine/in
ADP + phosphate + cyclobenzaprine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cyclobenzaprine/in
ADP + phosphate + cyclobenzaprine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + cycloheximide/in
ADP + phosphate + cycloheximide/out
-
Substrates: recombinant Cdr1p
Products: -
Products: -
?
ATP + H2O + cycloheximide/in
ADP + phosphate + cycloheximide/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + cycloheximide/in
ADP + phosphate + cycloheximide/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + cycloheximide[side 1]
ADP + phosphate + cycloheximide[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + cycloheximide[side 1]
ADP + phosphate + cycloheximide[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + cyclosporin A/in
ADP + phosphate + cyclosporin A/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + cyclosporin A/in
ADP + phosphate + cyclosporin A/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + cyclosporin A/in
ADP + phosphate + cyclosporin A/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + cyclosporin A/in
ADP + phosphate + cyclosporin A/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + cyclosporine A[side 1]
ADP + phosphate + cyclosporine A[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + cyclosporine A[side 1]
ADP + phosphate + cyclosporine A[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + cytarabine[side 1]
ADP + phosphate + cytarabine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + cytarabine[side 1]
ADP + phosphate + cytarabine[side 2]
Substrates: substrate for ABCC10
Products: -
Products: -
?
ATP + H2O + cytarabine[side 1]
ADP + phosphate + cytarabine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + daunomycin/in
ADP + phosphate + daunomycin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunomycin/in
ADP + phosphate + daunomycin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunomycin/in
ADP + phosphate + daunomycin/out
Substrates: YdaG/YdbA heterodimer
Products: -
Products: -
?
ATP + H2O + daunomycin/in
ADP + phosphate + daunomycin/out
Substrates: YdaG/YdbA heterodimer
Products: -
Products: -
?
ATP + H2O + daunomycin/in
ADP + phosphate + daunomycin/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + daunorubicin/in
ADP + phosphate + daunorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin/in
ADP + phosphate + daunorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin/in
ADP + phosphate + daunorubicin/out
-
Substrates: fluorescent substrate of P-glycoprotein
Products: -
Products: -
?
ATP + H2O + daunorubicin/in
ADP + phosphate + daunorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin/in
ADP + phosphate + daunorubicin/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin/in
ADP + phosphate + daunorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin/in
ADP + phosphate + daunorubicin/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin/in
ADP + phosphate + daunorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin/in
ADP + phosphate + daunorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin[side 1]
ADP + phosphate + daunorubicin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin[side 1]
ADP + phosphate + daunorubicin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin[side 1]
ADP + phosphate + daunorubicin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin[side 1]
ADP + phosphate + daunorubicin[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + daunorubicin[side 1]
ADP + phosphate + daunorubicin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + daunorubicin[side 1]
ADP + phosphate + daunorubicin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + daunorubicin[side 1]
ADP + phosphate + daunorubicin[side 2]
Substrates: substrate for P-glycoprotein and BCRP
Products: -
Products: -
?
ATP + H2O + daunorubicin[side 1]
ADP + phosphate + daunorubicin[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + deoxycholate[side 1]
ADP + phosphate + deoxycholate[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + deoxycholate[side 1]
ADP + phosphate + deoxycholate[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + diazepam/in
ADP + phosphate + diazepam/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + diazepam/in
ADP + phosphate + diazepam/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + diltiazem/in
ADP + phosphate + diltiazem/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + diltiazem/in
ADP + phosphate + diltiazem/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + diltiazem/in
ADP + phosphate + diltiazem/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + diltiazem/in
ADP + phosphate + diltiazem/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + diltiazem/in
ADP + phosphate + diltiazem/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin/in
ADP + phosphate + doxorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin/in
ADP + phosphate + doxorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin/in
ADP + phosphate + doxorubicin/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin/in
ADP + phosphate + doxorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin/in
ADP + phosphate + doxorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin/in
ADP + phosphate + doxorubicin/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
-
Substrates: poor transport by isoform Abcb5 compared to Abcb4
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
Substrates: substrate for P-glycoprotein, BCRP, and MRP1
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
Substrates: substrate for P-glycoprotein, BCRP, and MPR2
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin[side 1]
ADP + phosphate + doxorubicin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + erythromycin[side 1]
ADP + phosphate + erythromycin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + erythromycin[side 1]
ADP + phosphate + erythromycin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + estrone-3-sulfate/in
ADP + phosphate + estrone-3-sulfate/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + estrone-3-sulfate/in
ADP + phosphate + estrone-3-sulfate/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + estrone-3-sulfate[side 1]
ADP + phosphate + estrone-3-sulfate[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + estrone-3-sulfate[side 1]
ADP + phosphate + estrone-3-sulfate[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + estrone-3-sulfate[side 1]
ADP + phosphate + estrone-3-sulfate[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + ethanol/in
ADP + phosphate + ethanol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + ethanol/in
ADP + phosphate + ethanol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + ethidium bromide/in
ADP + phosphate + ethidium bromide/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + ethidium bromide/in
ADP + phosphate + ethidium bromide/out
-
Substrates: recombinant LmrA, expressed in Escherichia coli WD2
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ATP + H2O + ethidium bromide/in
ADP + phosphate + ethidium bromide/out
Substrates: YdaG/YdbA heterodimer
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ATP + H2O + ethidium bromide/in
ADP + phosphate + ethidium bromide/out
Substrates: YdaG/YdbA heterodimer
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ATP + H2O + ethidium bromide/in
ADP + phosphate + ethidium bromide/out
-
Substrates: -
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ATP + H2O + ethidium bromide/in
ADP + phosphate + ethidium bromide/out
Substrates: -
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ATP + H2O + ethidium bromide[side 1]
ADP + phosphate + ethidium bromide[side 2]
Substrates: -
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ATP + H2O + ethidium bromide[side 1]
ADP + phosphate + ethidium bromide[side 2]
Substrates: -
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ATP + H2O + ethidium bromide[side 1]
ADP + phosphate + ethidium bromide[side 2]
Substrates: -
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ATP + H2O + ethidium bromide[side 1]
ADP + phosphate + ethidium bromide[side 2]
Substrates: -
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ATP + H2O + ethidium bromide[side 1]
ADP + phosphate + ethidium bromide[side 2]
Planococcus maritimus DS 17275T
Substrates: -
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ATP + H2O + ethidium bromide[side 1]
ADP + phosphate + ethidium bromide[side 2]
-
Substrates: -
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ATP + H2O + ethidium[side 1]
ADP + phosphate + ethidium[side 2]
-
Substrates: -
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ATP + H2O + ethidium[side 1]
ADP + phosphate + ethidium[side 2]
-
Substrates: -
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ATP + H2O + ethidium[side 1]
ADP + phosphate + ethidium[side 2]
-
Substrates: -
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ATP + H2O + ethidium[side 1]
ADP + phosphate + ethidium[side 2]
-
Substrates: the wild type enzyme shows two translocation pathways with H+ or H+/Na+ antiport
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ATP + H2O + etoposide/in
ADP + phosphate + etoposide/out
-
Substrates: -
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ATP + H2O + etoposide/in
ADP + phosphate + etoposide/out
Substrates: -
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ATP + H2O + etoposide/in
ADP + phosphate + etoposide/out
-
Substrates: -
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ATP + H2O + etoposide[side 1]
ADP + phosphate + etoposide[side 2]
-
Substrates: -
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ATP + H2O + etoposide[side 1]
ADP + phosphate + etoposide[side 2]
Substrates: -
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ATP + H2O + etoposide[side 1]
ADP + phosphate + etoposide[side 2]
Substrates: substrate for MRP1
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ATP + H2O + etoposide[side 1]
ADP + phosphate + etoposide[side 2]
Substrates: substrate for P-glycoprotein, BCRP, and MPR2
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ATP + H2O + etoposide[side 1]
ADP + phosphate + etoposide[side 2]
-
Substrates: -
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ATP + H2O + etoposide[side 1]
ADP + phosphate + etoposide[side 2]
Substrates: -
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ATP + H2O + fluconazole/in
ADP + phosphate + fluconazole/out
-
Substrates: recombinant Cdr1p
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ATP + H2O + fluconazole/in
ADP + phosphate + fluconazole/out
-
Substrates: -
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ATP + H2O + fluconazole/in
ADP + phosphate + fluconazole/out
-
Substrates: -
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ATP + H2O + fluoxetine/in
ADP + phosphate + fluoxetine/out
-
Substrates: -
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ATP + H2O + fluoxetine/in
ADP + phosphate + fluoxetine/out
-
Substrates: -
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ATP + H2O + fluvoxamine/in
ADP + phosphate + fluvoxamine/out
-
Substrates: -
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ATP + H2O + fluvoxamine/in
ADP + phosphate + fluvoxamine/out
-
Substrates: -
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ATP + H2O + furosemide/in
ADP + phosphate + furosemide/out
-
Substrates: good substrate for MRP3, but not for MRP1
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ATP + H2O + furosemide/in
ADP + phosphate + furosemide/out
-
Substrates: -
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ATP + H2O + gefitinib[side 1]
ADP + phosphate + gefitinib[side 2]
Substrates: substrate for BCRP
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ATP + H2O + gefitinib[side 1]
ADP + phosphate + gefitinib[side 2]
Substrates: substrate for P-glycoprotein and BCRP
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ATP + H2O + genistein[side 1]
ADP + phosphate + genistein[side 2]
Substrates: substrate for BCRP
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ATP + H2O + genistein[side 1]
ADP + phosphate + genistein[side 2]
Substrates: substrate for P-glycoprotein
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ATP + H2O + gentamicin[side 1]
ADP + phosphate + gentamicin[side 2]
-
Substrates: -
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ATP + H2O + gentamicin[side 1]
ADP + phosphate + gentamicin[side 2]
Substrates: -
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ATP + H2O + Hoechst 33342/in
ADP + phosphate + Hoechst 33342/out
-
Substrates: -
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ATP + H2O + Hoechst 33342/in
ADP + phosphate + Hoechst 33342/out
-
Substrates: -
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ATP + H2O + Hoechst 33342/in
ADP + phosphate + Hoechst 33342/out
-
Substrates: -
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ATP + H2O + Hoechst 33342/in
ADP + phosphate + Hoechst 33342/out
Substrates: -
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ATP + H2O + Hoechst 33342[side 1]
ADP + phosphate + Hoechst 33342[side 2]
-
Substrates: -
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ATP + H2O + Hoechst 33342[side 1]
ADP + phosphate + Hoechst 33342[side 2]
-
Substrates: -
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ATP + H2O + Hoechst 33342[side 1]
ADP + phosphate + Hoechst 33342[side 2]
Substrates: substrate for P-glycoprotein
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ATP + H2O + Hoechst 33342[side 1]
ADP + phosphate + Hoechst 33342[side 2]
Substrates: -
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ATP + H2O + Hoechst 33342[side 1]
ADP + phosphate + Hoechst 33342[side 2]
Substrates: -
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ATP + H2O + Hoechst33342[side 1]
ADP + phosphate + Hoechst33342[side 2]
Substrates: -
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ATP + H2O + Hoechst33342[side 1]
ADP + phosphate + Hoechst33342[side 2]
Substrates: -
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ATP + H2O + Hoechst33342[side 1]
ADP + phosphate + Hoechst33342[side 2]
Substrates: -
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ATP + H2O + Hoechst33342[side 1]
ADP + phosphate + Hoechst33342[side 2]
-
Substrates: -
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ATP + H2O + Hoechst33342[side 1]
ADP + phosphate + Hoechst33342[side 2]
-
Substrates: -
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ATP + H2O + hydroxyzine/in
ADP + phosphate + hydroxyzine/out
-
Substrates: -
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ATP + H2O + hydroxyzine/in
ADP + phosphate + hydroxyzine/out
-
Substrates: -
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ATP + H2O + indinavir[side 1]
ADP + phosphate + indinavir[side 2]
Substrates: substrate for P-glycoprotein
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ATP + H2O + indinavir[side 1]
ADP + phosphate + indinavir[side 2]
Substrates: substrate for P-glycoprotein
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ATP + H2O + indinavir[side 1]
ADP + phosphate + indinavir[side 2]
Substrates: substrate for MPR2
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ATP + H2O + indomethacin/in
ADP + phosphate + indomethacin/out
-
Substrates: moderate substrate for MRP1, weak substrate for MRP3
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ATP + H2O + indomethacin/in
ADP + phosphate + indomethacin/out
-
Substrates: -
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ATP + H2O + iodoarylazidoprazosin[side 1]
ADP + phosphate + iodoarylazidoprazosin[side 2]
Substrates: -
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ATP + H2O + iodoarylazidoprazosin[side 1]
ADP + phosphate + iodoarylazidoprazosin[side 2]
-
Substrates: -
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ATP + H2O + kanamycin[side 1]
ADP + phosphate + kanamycin[side 2]
-
Substrates: -
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ATP + H2O + kanamycin[side 1]
ADP + phosphate + kanamycin[side 2]
Substrates: -
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ATP + H2O + ketoconazole/in
ADP + phosphate + ketoconazole/out
-
Substrates: -
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ATP + H2O + ketoconazole/in
ADP + phosphate + ketoconazole/out
-
Substrates: substrate from a ethyl acetate extract of Trichilia emetica leaves and seeds
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ATP + H2O + ketoconazole/in
ADP + phosphate + ketoconazole/out
-
Substrates: -
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ATP + H2O + ketoconazole/in
ADP + phosphate + ketoconazole/out
-
Substrates: substrate from a ethyl acetate extract of Trichilia emetica leaves and seeds
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ATP + H2O + ketoconazole/in
ADP + phosphate + ketoconazole/out
-
Substrates: substrate from a ethyl acetate extract of Trichilia emetica leaves and seeds
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ATP + H2O + ketoconazole/in
ADP + phosphate + ketoconazole/out
Nakaseomyces glabratus CCM8270
-
Substrates: substrate from a ethyl acetate extract of Trichilia emetica leaves and seeds
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ATP + H2O + ketoconazole[side 1]
ADP + phosphate + ketoconazole[side 2]
Substrates: substrate for P-glycoprotein
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ATP + H2O + ketoconazole[side 1]
ADP + phosphate + ketoconazole[side 2]
-
Substrates: -
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ATP + H2O + ketoconazole[side 1]
ADP + phosphate + ketoconazole[side 2]
-
Substrates: the enzyme shows highest efficiency for ATP
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ATP + H2O + ketoconazole[side 1]
ADP + phosphate + ketoconazole[side 2]
-
Substrates: -
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ATP + H2O + ketoconazole[side 1]
ADP + phosphate + ketoconazole[side 2]
Saccharomyces cerevisiae YRE1001
-
Substrates: the enzyme shows highest efficiency for ATP
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ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: high activity with
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ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: natural substrate of MRP1
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ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: natural substrate of MRP1, ATP-stimulated LTC4 uptake of Sf9 inside-out membrane vesicles, roles of the highly conserved ABC-signature regions in the two non-equivalent ABC units of MRP1, major functional role of the conserved glycine residues in both ABC units of MRP1 and formation of composite catalytically active sites involving both signature regions within the ABC domains
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ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: -
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ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: glutathione is not required
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ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: -
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ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: -
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ATP + H2O + leukotriene C4[side 1]
ADP + phosphate + leukotriene C4[side 2]
Substrates: substrate for MRP1
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ATP + H2O + leukotriene C4[side 1]
ADP + phosphate + leukotriene C4[side 2]
-
Substrates: -
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ATP + H2O + Lipid A/in
ADP + phosphate + Lipid A/out
-
Substrates: native LmrA
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ATP + H2O + Lipid A/in
ADP + phosphate + Lipid A/out
-
Substrates: native LmrA
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ATP + H2O + loperamide/in
ADP + phosphate + loperamide/out
-
Substrates: -
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ATP + H2O + loperamide/in
ADP + phosphate + loperamide/out
-
Substrates: -
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ATP + H2O + lopinavir[side 1]
ADP + phosphate + lopinavir[side 2]
Substrates: substrate for P-glycoprotein
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ATP + H2O + lopinavir[side 1]
ADP + phosphate + lopinavir[side 2]
Substrates: substrate for MPR2 and BCRP
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ATP + H2O + methotrexate/in
ADP + phosphate + methotrexate/out
-
Substrates: -
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ATP + H2O + methotrexate/in
ADP + phosphate + methotrexate/out
-
Substrates: -
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ATP + H2O + methotrexate/in
ADP + phosphate + methotrexate/out
-
Substrates: -
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ATP + H2O + methotrexate[side 1]
ADP + phosphate + methotrexate[side 2]
Substrates: substrate for BCRP
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ATP + H2O + methotrexate[side 1]
ADP + phosphate + methotrexate[side 2]
Substrates: substrate for ABCG2
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ATP + H2O + methotrexate[side 1]
ADP + phosphate + methotrexate[side 2]
Substrates: -
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ATP + H2O + methotrexate[side 1]
ADP + phosphate + methotrexate[side 2]
Substrates: substrate for ABCC4
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ATP + H2O + methotrexate[side 1]
ADP + phosphate + methotrexate[side 2]
Substrates: substrate for P-glycoprotein, BCRP, and MPR2
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ATP + H2O + methotrexate[side 1]
ADP + phosphate + methotrexate[side 2]
Substrates: -
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ATP + H2O + methotrexate[side 1]
ADP + phosphate + methotrexate[side 2]
Substrates: -
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ATP + H2O + methyl viologen[side 1]
ADP + phosphate + methyl viologen[side 2]
Substrates: -
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ATP + H2O + methyl viologen[side 1]
ADP + phosphate + methyl viologen[side 2]
Substrates: -
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ATP + H2O + miconazole/in
ADP + phosphate + miconazole/out
-
Substrates: recombinant Cdr1p
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ATP + H2O + miconazole/in
ADP + phosphate + miconazole/out
-
Substrates: -
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ATP + H2O + miconazolenitrate[side 1]
ADP + phosphate + miconazolenitrate[side 2]
-
Substrates: -
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ATP + H2O + miconazolenitrate[side 1]
ADP + phosphate + miconazolenitrate[side 2]
-
Substrates: -
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ATP + H2O + midazolam/in
ADP + phosphate + midazolam/out
-
Substrates: -
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ATP + H2O + midazolam/in
ADP + phosphate + midazolam/out
-
Substrates: -
Products: -
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ATP + H2O + mitomycin C[side 1]
ADP + phosphate + mitomycin C[side 2]
Substrates: substrate for P-glycoprotein
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ATP + H2O + mitomycin C[side 1]
ADP + phosphate + mitomycin C[side 2]
Substrates: substrate for P-glycoprotein
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ATP + H2O + mitoxantrone[side 1]
ADP + phosphate + mitoxantrone[side 2]
-
Substrates: poor transport by isoform Abcb5 compared to Abcb4
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ATP + H2O + mitoxantrone[side 1]
ADP + phosphate + mitoxantrone[side 2]
Substrates: substrate for BCRP
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ATP + H2O + mitoxantrone[side 1]
ADP + phosphate + mitoxantrone[side 2]
Substrates: -
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ATP + H2O + mitoxantrone[side 1]
ADP + phosphate + mitoxantrone[side 2]
Substrates: substrate for P-glycoprotein, BCRP, and MPR2
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ATP + H2O + mitoxantrone[side 1]
ADP + phosphate + mitoxantrone[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + mitoxantrone[side 1]
ADP + phosphate + mitoxantrone[side 2]
Substrates: -
Products: -
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?
ATP + H2O + N-benzyl-2-nitro-1H-imidazole-1-acetamide/in
ADP + phosphate + N-benzyl-2-nitro-1H-imidazole-1-acetamide/out
-
Substrates: -
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ATP + H2O + N-benzyl-2-nitro-1H-imidazole-1-acetamide/in
ADP + phosphate + N-benzyl-2-nitro-1H-imidazole-1-acetamide/out
-
Substrates: -
Products: -
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ATP + H2O + N-ethylmaleimide S-glutathione/in
ADP + phosphate + N-ethylmaleimide S-glutathione/out
-
Substrates: NEM-GS is a good substrate for MRP1, but not for MRP3
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ATP + H2O + N-ethylmaleimide S-glutathione/in
ADP + phosphate + N-ethylmaleimide S-glutathione/out
-
Substrates: roles of the highly conserved ABC-signature regions in the two non-equivalent ABC units of MRP1, major functional role of the conserved glycine residues in both ABC units of MRP1 and formation of composite catalytically active sites involving both signature regions within the ABC domains
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ATP + H2O + N-ethylmaleimide S-glutathione/in
ADP + phosphate + N-ethylmaleimide S-glutathione/out
-
Substrates: -
Products: -
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?
ATP + H2O + nelfinavir[side 1]
ADP + phosphate + nelfinavir[side 2]
Substrates: substrate for P-glycoprotein
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?
ATP + H2O + nelfinavir[side 1]
ADP + phosphate + nelfinavir[side 2]
Substrates: substrate for MPR2 and BCRP
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?
ATP + H2O + nicardipine[side 1]
ADP + phosphate + nicardipine[side 2]
Substrates: -
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?
ATP + H2O + nicardipine[side 1]
ADP + phosphate + nicardipine[side 2]
Substrates: -
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?
ATP + H2O + nicardipine[side 1]
ADP + phosphate + nicardipine[side 2]
Substrates: substrate for BCRP
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?
ATP + H2O + norfloxacin[side 1]
ADP + phosphate + norfloxacin[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + norfloxacin[side 1]
ADP + phosphate + norfloxacin[side 2]
Substrates: -
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?
ATP + H2O + norfloxacin[side 1]
ADP + phosphate + norfloxacin[side 2]
Substrates: substrate for BCRP
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?
ATP + H2O + norfloxacin[side 1]
ADP + phosphate + norfloxacin[side 2]
Substrates: -
Products: -
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?
ATP + H2O + norfloxacin[side 1]
ADP + phosphate + norfloxacin[side 2]
Planococcus maritimus DS 17275T
Substrates: -
Products: -
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?
ATP + H2O + norfloxacin[side 1]
ADP + phosphate + norfloxacin[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + nortryptiline/in
ADP + phosphate + nortryptiline/out
-
Substrates: -
Products: -
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?
ATP + H2O + nortryptiline/in
ADP + phosphate + nortryptiline/out
-
Substrates: -
Products: -
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?
ATP + H2O + ochratoxin A[side 1]
ADP + phosphate + ochratoxin A[side 2]
Substrates: -
Products: -
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?
ATP + H2O + ochratoxin A[side 1]
ADP + phosphate + ochratoxin A[side 2]
Substrates: -
Products: -
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?
ATP + H2O + ofloxacin[side 1]
ADP + phosphate + ofloxacin[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + ofloxacin[side 1]
ADP + phosphate + ofloxacin[side 2]
Substrates: -
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?
ATP + H2O + ofloxacin[side 1]
ADP + phosphate + ofloxacin[side 2]
Substrates: substrate for BCRP
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?
ATP + H2O + p-methoxy-ethylamphetamine/in
ADP + phosphate + p-methoxy-ethylamphetamine/out
-
Substrates: -
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?
ATP + H2O + p-methoxy-ethylamphetamine/in
ADP + phosphate + p-methoxy-ethylamphetamine/out
-
Substrates: cell resistance against the drug substrate is diminished by ATP depletion and enzyme inhibition
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?
ATP + H2O + p-methoxy-ethylamphetamine/in
ADP + phosphate + p-methoxy-ethylamphetamine/out
-
Substrates: -
Products: -
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?
ATP + H2O + paclitaxel/in
ADP + phosphate + paclitaxel/out
Substrates: -
Products: -
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?
ATP + H2O + paclitaxel/in
ADP + phosphate + paclitaxel/out
-
Substrates: -
Products: -
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?
ATP + H2O + paclitaxel/in
ADP + phosphate + paclitaxel/out
Substrates: -
Products: -
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?
ATP + H2O + paclitaxel/in
ADP + phosphate + paclitaxel/out
-
Substrates: -
Products: -
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?
ATP + H2O + paclitaxel[side 1]
ADP + phosphate + paclitaxel[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + paclitaxel[side 1]
ADP + phosphate + paclitaxel[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + paroxetine/in
ADP + phosphate + paroxetine/out
-
Substrates: -
Products: -
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?
ATP + H2O + paroxetine/in
ADP + phosphate + paroxetine/out
-
Substrates: -
Products: -
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?
ATP + H2O + prazosin/in
ADP + phosphate + prazosin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + prazosin/in
ADP + phosphate + prazosin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + prednisone/in
ADP + phosphate + prednisone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + prednisone/in
ADP + phosphate + prednisone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + probenecid/in
ADP + phosphate + probenecid/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + probenecid/in
ADP + phosphate + probenecid/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + progesterone/in
ADP + phosphate + progesterone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + progesterone/in
ADP + phosphate + progesterone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + progesterone/in
ADP + phosphate + progesterone/out
-
Substrates: P-gp substrate
Products: -
Products: -
?
ATP + H2O + progesterone/in
ADP + phosphate + progesterone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + propoxyphene/in
ADP + phosphate + propoxyphene/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + propoxyphene/in
ADP + phosphate + propoxyphene/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + quercetin[side 1]
ADP + phosphate + quercetin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + quercetin[side 1]
ADP + phosphate + quercetin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + quercetin[side 1]
ADP + phosphate + quercetin[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + quinidine/in
ADP + phosphate + quinidine/out
-
Substrates: affinity of qunidine to MDR1 is higher at pH 7.4 than at pH 6.8. Protein concentration is inversely related to the maximum activation of ATPase activity achieved
Products: -
Products: -
?
ATP + H2O + quinidine/in
ADP + phosphate + quinidine/out
-
Substrates: EC50 value 0.0164 mM
Products: -
Products: -
?
ATP + H2O + quinidine/in
ADP + phosphate + quinidine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + quinidine/in
ADP + phosphate + quinidine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + quinidine[side 1]
ADP + phosphate + quinidine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + quinidine[side 1]
ADP + phosphate + quinidine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + quinidine[side 1]
ADP + phosphate + quinidine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + resazurine/in
ADP + phosphate + resazurine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + resazurine/in
ADP + phosphate + resazurine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + resorufine/in
ADP + phosphate + resorufine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + resorufine/in
ADP + phosphate + resorufine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: less efficient substrate than tetramethylrosamine
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: the enzyme plays an important role in drug resistance
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: fluorescent substrate
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123[side 1]
ADP + phosphate + rhodamine 123[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123[side 1]
ADP + phosphate + rhodamine 123[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123[side 1]
ADP + phosphate + rhodamine 123[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + rhodamine 123[side 1]
ADP + phosphate + rhodamine 123[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + rhodamine 123[side 1]
ADP + phosphate + rhodamine 123[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123[side 1]
ADP + phosphate + rhodamine 123[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 123[side 1]
ADP + phosphate + rhodamine 123[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 6 G[side 1]
ADP + phosphate + rhodamine 6 G[side 2]
-
Substrates: the enzyme shows highest efficiency for ATP
Products: -
Products: -
?
ATP + H2O + rhodamine 6 G[side 1]
ADP + phosphate + rhodamine 6 G[side 2]
Saccharomyces cerevisiae YRE1001
-
Substrates: the enzyme shows highest efficiency for ATP
Products: -
Products: -
?
ATP + H2O + rhodamine 6G/in
ADP + phosphate + rhodamine 6G/out
-
Substrates: recombinant Cdr1p
Products: -
Products: -
?
ATP + H2O + rhodamine 6G/in
ADP + phosphate + rhodamine 6G/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 6G/in
ADP + phosphate + rhodamine 6G/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 6G/in
ADP + phosphate + rhodamine 6G/out
-
Substrates: substrate for Snq2p and Pdr5p
Products: -
Products: -
?
ATP + H2O + rhodamine 6G[side 1]
ADP + phosphate + rhodamine 6G[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 6G[side 1]
ADP + phosphate + rhodamine 6G[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 6G[side 1]
ADP + phosphate + rhodamine 6G[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 6G[side 1]
ADP + phosphate + rhodamine 6G[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine 6G[side 1]
ADP + phosphate + rhodamine 6G[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine B[side 1]
ADP + phosphate + rhodamine B[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + rhodamine B[side 1]
ADP + phosphate + rhodamine B[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + riboflavin[side 1]
ADP + phosphate + riboflavin[side 2]
Substrates: substrate for BCRP
Products: -
Products: -
?
ATP + H2O + riboflavin[side 1]
ADP + phosphate + riboflavin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + rifampicin[side 1]
ADP + phosphate + rifampicin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + rifampicin[side 1]
ADP + phosphate + rifampicin[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + rifampicin[side 1]
ADP + phosphate + rifampicin[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + risperidone/in
ADP + phosphate + risperidone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + risperidone/in
ADP + phosphate + risperidone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + ritonavir/in
ADP + phosphate + ritonavir/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + ritonavir/in
ADP + phosphate + ritonavir/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + ritonavir/in
ADP + phosphate + ritonavir/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + ritonavir[side 1]
ADP + phosphate + ritonavir[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + ritonavir[side 1]
ADP + phosphate + ritonavir[side 2]
Substrates: substrate for P-glycoprotein and MRP1
Products: -
Products: -
?
ATP + H2O + ritonavir[side 1]
ADP + phosphate + ritonavir[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + ritonavir[side 1]
ADP + phosphate + ritonavir[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + ritonavir[side 1]
ADP + phosphate + ritonavir[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + S-2,4-dinitrophenylglutathione/in
ADP + phosphate + S-2,4-dinitrophenylglutathione/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + S-2,4-dinitrophenylglutathione/in
ADP + phosphate + S-2,4-dinitrophenylglutathione/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + S-2,4-dinitrophenylglutathione/in
ADP + phosphate + S-2,4-dinitrophenylglutathione/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + saquinavir[side 1]
ADP + phosphate + saquinavir[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + saquinavir[side 1]
ADP + phosphate + saquinavir[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + saquinavir[side 1]
ADP + phosphate + saquinavir[side 2]
Substrates: substrate for MPR2
Products: -
Products: -
?
ATP + H2O + saquinavir[side 1]
ADP + phosphate + saquinavir[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + sertraline/in
ADP + phosphate + sertraline/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + sertraline/in
ADP + phosphate + sertraline/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + SN-38[side 1]
ADP + phosphate + SN-38[side 2]
Substrates: SN-38 is 7-ethyl-10-hydroxy-CPT
Products: -
Products: -
?
ATP + H2O + SN-38[side 1]
ADP + phosphate + SN-38[side 2]
Substrates: substrate for MPR2 and BCRP
Products: -
Products: -
?
ATP + H2O + streptomycin[side 1]
ADP + phosphate + streptomycin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + streptomycin[side 1]
ADP + phosphate + streptomycin[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + tamoxifen[side 1]
ADP + phosphate + tamoxifen[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + tamoxifen[side 1]
ADP + phosphate + tamoxifen[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + taurocholic acid[side 1]
ADP + phosphate + taurocholic acid[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + taurocholic acid[side 1]
ADP + phosphate + taurocholic acid[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + taxol[side 1]
ADP + phosphate + taxol[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + taxol[side 1]
ADP + phosphate + taxol[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + teniposide[side 1]
ADP + phosphate + teniposide[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + teniposide[side 1]
ADP + phosphate + teniposide[side 2]
Substrates: substrate for P-glycoprotein and BCRP
Products: -
Products: -
?
ATP + H2O + tetracycline[side 1]
ADP + phosphate + tetracycline[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + tetracycline[side 1]
ADP + phosphate + tetracycline[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + tetracycline[side 1]
ADP + phosphate + tetracycline[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + tetramethylrosamine/in
ADP + phosphate + tetramethylrosamine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + tetramethylrosamine/in
ADP + phosphate + tetramethylrosamine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + tetraphenylphosphonium[side 1]
ADP + phosphate + tetraphenylphosphonium[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + tetraphenylphosphonium[side 1]
ADP + phosphate + tetraphenylphosphonium[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + tetraphenylphosphonium[side 1]
ADP + phosphate + tetraphenylphosphonium[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + topotecan[side 1]
ADP + phosphate + topotecan[side 2]
Substrates: substrate for P-glycoprotein and BCRP
Products: -
Products: -
?
ATP + H2O + topotecan[side 1]
ADP + phosphate + topotecan[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + topotecan[side 1]
ADP + phosphate + topotecan[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + trans-resveratrol[side 1]
ADP + phosphate + trans-resveratrol[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + trans-resveratrol[side 1]
ADP + phosphate + trans-resveratrol[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + trazodone/in
ADP + phosphate + trazodone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + trazodone/in
ADP + phosphate + trazodone/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Triton X-100/in
ADP + phosphate + Triton X-100/out
Substrates: above the critical micellar concentration, Triton X-100 leads to a rapid and irreversible decrease in extracellular acidification rate in both, wild-type and transfected cells which is due to cell lysis
Products: -
Products: -
?
ATP + H2O + Triton X-100/in
ADP + phosphate + Triton X-100/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Tween 80/in
ADP + phosphate + Tween 80/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + Tween 80/in
ADP + phosphate + Tween 80/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + urate/in
ADP + phosphate + urate/out
-
Substrates: MRP4 is the first secretory transporter identified in the bidirectional renal handling of urate and could be a potential drug target in the treatment of hyperuricaemia, regulation, overview
Products: -
Products: -
?
ATP + H2O + valinomycin/in
ADP + phosphate + valinomycin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + valinomycin/in
ADP + phosphate + valinomycin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: P-gp substrate
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: EPR spin-labeled verapamil is an excellent transport substrate, the affinity is 10fold higher than for unlabeled verapamil
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: unlabeled and spin-labeled verapamil
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: affinity of verapamil to MDR1 is higher at pH 7.4 than at pH 6.8. Protein concentration is inversely related to the maximum activation of ATPase activity achieved
Products: affinity of verapamil to MDR1 is higher at pH 7.4 than at pH 6.8. Protein concentration is inversely related to the maximum activation of ATPase activity achieved
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: EC50 value 0.00285 mM
Products: EC50 value 0.00285 mM
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil[side 1]
ADP + phosphate + verapamil[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil[side 1]
ADP + phosphate + verapamil[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil[side 1]
ADP + phosphate + verapamil[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil[side 1]
ADP + phosphate + verapamil[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + verapamil[side 1]
ADP + phosphate + verapamil[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + verapamil[side 1]
ADP + phosphate + verapamil[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + verapamil[side 1]
ADP + phosphate + verapamil[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine/in
ADP + phosphate + vinblastine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine/in
ADP + phosphate + vinblastine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine/in
ADP + phosphate + vinblastine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine/in
ADP + phosphate + vinblastine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine/in
ADP + phosphate + vinblastine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine/in
ADP + phosphate + vinblastine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine/in
ADP + phosphate + vinblastine/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine[side 1]
ADP + phosphate + vinblastine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine[side 1]
ADP + phosphate + vinblastine[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine[side 1]
ADP + phosphate + vinblastine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine[side 1]
ADP + phosphate + vinblastine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine[side 1]
ADP + phosphate + vinblastine[side 2]
Substrates: substrate for P-glycoprotein
Products: -
Products: -
?
ATP + H2O + vinblastine[side 1]
ADP + phosphate + vinblastine[side 2]
Substrates: substrate for P-glycoprotein and MPR2
Products: -
Products: -
?
ATP + H2O + vinblastine[side 1]
ADP + phosphate + vinblastine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine[side 1]
ADP + phosphate + vinblastine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine[side 1]
ADP + phosphate + vinblastine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + vinblastine[side 1]
ADP + phosphate + vinblastine[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + vincristine[side 1]
ADP + phosphate + vincristine[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + vincristine[side 1]
ADP + phosphate + vincristine[side 2]
Substrates: substrate for P-glycoprotein
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Products: -
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ATP + H2O + vincristine[side 1]
ADP + phosphate + vincristine[side 2]
Substrates: substrate for P-glycoprotein and MPR2
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ATP + H2O + vincristine[side 1]
ADP + phosphate + vincristine[side 2]
Substrates: -
Products: -
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ATP + H2O + VP-16/in
ADP + phosphate + VP-16/out
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: multidrug ABC transporter YvcC, the high ATP hydrolysis proceeds via a positive cooperativity mechanism, two drug binding sites coexist on YvcC
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: the enzyme forms stable, highly ordered ring-shaped structures, that are destroyed or whose formation is prevented upon addition of ATP in the presence of Mg2+ and the subsequent catalytic step responsible for such an effect, overview
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: ABC multidrug transporter Cdr1p, domain structure, roles of Cys-193 of the Walker A motif of the N-terminal nucleotide binding domain and of Lys-901 of the Walker A motif of the C-terminal nucleotide binding domain in ATPase function, the two nucleotide binding domains influence the Cdr1p function asymmetrically
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: importance of Candida drug resistance protein Cdr1p of pathogenic Candida albicans in azole resistance
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: the typical Cys193 in Walker A as well as Trp326 and Asp327 in the Walker B of N-terminal nucleotide binding domain of Cdr1p have acquired unique roles in ATP binding and hydrolysis. Asn328 is a gamma-phosphate sensor. ATP docking subsequent to Mg2+ coordination induces further conformational changes, structure analysis, overview
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: thermodynamic analysis of ATP hydrolysis in the presence and absence of transport substrates, mechanism
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: expression at the tumor cell surface of P-glycoprotein, which functions as an ATP-powered multidrug efflux pump, is involved in multidrug resistance. It also shows lipid flippase activity
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: multidrug resistance, the major physiological role is the protection of cells and tissues against xenobiotics, relevance of MRP1 and MRP3 proteins in chemoresistance of cancer and in drug metabolism and toxicity
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: MDR1, multiple drug resistance, ABC transporter, which acts as ATP-driven pump that removes xenobiotics from the interior of cells
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: ATP-driven pumping of a variety of drugs out of cells, multidrug resistance, hydrophobic model of drug transport by P-glycoprotein
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: wide substrate specificity of MDR proteins, MDR1 preferentially extrudes large hydrophobic, positively charged molecules, members of the MRP family extrudes both hydrophobic uncharged molecules and water-soluble anionic compounds
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: MDR1, ABC transporter, which acts as ATP-driven pump that removes xenobiotics from the interior of cells, uses a wide variety of substrates
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: P-gp catalyzes the ATP hydrolysis-dependent efflux of numerous amphiphilic compounds of unrelated chemical structures
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: mechanism, model of the MRP1 ATPase hydrolytic cycle, nucleotide-binding and MRP1 interaction with the transported substrates induce two different allosteric effects during the ATPase cycle, MRP1 domain structure
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: ATP-driven pumping of a variety of drugs out of cells, hydrophobic vacuum cleaner model of drug transport by P-glycoprotein
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: Pgp transports drugs out of cells, very broad specificity drug pump, thermodynamic analysis of ATP hydrolysis in the presence and absence of transport substrates, mechanism, model of drug transport
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: P-glycoprotein is a membrane ATP-driven drug exporter, Pgp actively extrudes a spectrum of hydrophobic xenobiotics, including a number of anticancer drugs
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: MRP1 transports a wide range of natural product drugs and structurally diverse conjugated and unconjugated organic anions. Its closest relative is MRP3. MRP1 transports GSH and GSH conjugates and displays GSH-stimulated transport of a number of unconjugated and conjugated compounds. In contrast, MRP3 does not transport GSH and is a poor transporter of GSH conjugates
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: the P-glycoprotein mediates multidrug resistance, which can be overcome by enzyme inhibition and ATP depletion allowing drug containing nanoparticles to target both drug and biological mechanisms
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: multidrug resistance protein MDR1, i.e. P-glycoprotein or ABCB1, is an ATP-dependent efflux pump for various cytotoxic agents, and is implicated in the resistance of human tumors to chemotherapeutic drugs
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: MRP4 limits brain entry and promotes renal excretion of drugs. In addition to its role in the body distribution and renal excretion of a wide variety of antiviral, cytostatic, antibiotic and cardiovascular drugs, MRP4/ABCC4 has the ability to transport molecules involved in cellular signalling. These molecules include cyclic nucleotides, eicosanoids, urate and conjugated steroids. The unique structure, regulation and dual localisation of MRP4 in polarised cells could be connected with a key function in cellular protection and extracellular signalling pathways, overview
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: the enzyme increases the resistance level of cells against drugs, overview
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: P-gp 170 has two potentially interesting regions for drugs interfering with its efflux function, namely the oligosaccharides on the first extracellular loop with unknown function and the two intracellular ATP-binding regions providing the energy for drug efflux function. P-gp is a polytopic plasma membrane protein whose overexpression causes multidrug resistance, MDR, responsible for the failure of cancer chemotherapy
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: P-glycoprotein belongs to the family of ATP-binding cassette proteins which hydrolyze ATP to catalyse the translocation of their substrates through membranes
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: the ATP-binding cassette multidrug resistance protein 1 mediates ATP-dependent cellular efflux of drugs and organic anions
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: structure-activity relationship, overview
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: ATP-dependent transport into inside-out membrane vesicles by recombinant enzymes, overview
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: ATP-dependent MRP1-mediated uptake of labeled substrates in membrane vesicles
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: a cluster of aromatic residues located at the interface between the nucleotide binding domain and the transmembrane domain in opposite halves of the molecule may contribute to this signal transmission upon ATP binding and hydrolysis, binding and/or hydrolysis of ATP induce conformational changes that are transmitted from the nucleotide binding domains to the transmembrane domains, overview
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: functional importance of MRP1-Pro1150 at the interface of transmembrane helix 15 and cytoplasmic loop 7
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Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: ABC multidrug transporter LmrA, substrate specificity
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
Substrates: YdaG and YdbA are two ABC multidrug half-transporters, ATPase activity is associated with the YdaG/YdbA heterodimer only and not with the individual subunits
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
Substrates: YdaG and YdbA are two ABC multidrug half-transporters, ATPase activity is associated with the YdaG/YdbA heterodimer only and not with the individual subunits
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: ABC multidrug transporter LmrA, substrate specificity
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Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: in the brain, MRP4 limits the entry of drugs and is involved in nociception, probably as a result of reduced plasma prostaglandins. In the kidney, MRP4 mediates the active tubular secretion of diuretics, antiviral nucleosides and cephalosporins. In the liver, MRP4 mediates the efflux of bile acid to the blood, and knockout mice are more sensitive to cholestatic-induced liver injury. MRP4 protects bone marrow cells and the gastrointestinal tract against cytotoxic drugs and appears to be involved in secretory diarrhoea via coupling with CFTR
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
Nakaseomyces glabratus CCM8270
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: SMDR2 is an ATP-dependent efflux pump involved in transport of toxins and xenobiotics from cells
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
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ATP + H2O + zolpidem/in
ADP + phosphate + zolpidem/out
-
Substrates: -
Products: -
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ATP + H2O + zolpidem/in
ADP + phosphate + zolpidem/out
-
Substrates: -
Products: -
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cyclo(D-Trp-D-Asp-L-Pro-D-Val-L-Leu)/in + ATP + H2O
cyclo(D-Trp-D-Asp-L-Pro-D-Val-L-Leu)/out + ADP + phosphate
-
Substrates: no other common substrate detected
Products: -
Products: -
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cyclo(D-Trp-D-Asp-L-Pro-D-Val-L-Leu)/in + ATP + H2O
cyclo(D-Trp-D-Asp-L-Pro-D-Val-L-Leu)/out + ADP + phosphate
-
Substrates: no other common substrate detected
Products: -
Products: -
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daunorubicin/in + ATP + H2O
daunorubicin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
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daunorubicin/in + ATP + H2O
daunorubicin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
doxorubicin/in + ATP + H2O
doxorubicin/out + ADP + phosphate
-
Substrates: -
Products: -
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doxorubicin/in + ATP + H2O
doxorubicin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
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doxorubicin/in + ATP + H2O
doxorubicin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
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erythromycin/in + ATP + H2O
erythromycin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
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erythromycin/in + ATP + H2O
erythromycin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
estradiol 17-beta-D-glucuronide/in + ATP + H2O
estradiol 17-beta-D-glucuronide/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
estradiol 17-beta-D-glucuronide/in + ATP + H2O
estradiol 17-beta-D-glucuronide/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
etoposide/in + ATP + H2O
etoposide/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
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etoposide/in + ATP + H2O
etoposide/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
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leukotriene C4/in + ATP + H2O
leukotriene C4/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
leukotriene C4/in + ATP + H2O
leukotriene C4/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
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leukotriene C4/in + ATP + H2O
leukotriene C4/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
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leukotriene D4/in + ATP + H2O
leukotriene D4/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
leukotriene D4/in + ATP + H2O
leukotriene D4/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
oleandomycin/in + ATP + H2O
oleandomycin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
oleandomycin/in + ATP + H2O
oleandomycin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
rhodamine 123/in + ATP + H2O
rhodamine 123/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
rhodamine 123/in + ATP + H2O
rhodamine 123/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
S-(2,4-dinitrophenyl)glutathione/in + ATP + H2O
S-(2,4-dinitrophenyl)glutathione/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
S-(2,4-dinitrophenyl)glutathione/in + ATP + H2O
S-(2,4-dinitrophenyl)glutathione/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
spiramycin/in + ATP + H2O
spiramycin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
spiramycin/in + ATP + H2O
spiramycin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
tetracyclin/in + ATP + H2O
tetracyclin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
tetracyclin/in + ATP + H2O
tetracyclin/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
UTP + H2O + ketoconazole[side 1]
UDP + phosphate + ketoconazole[side 2]
-
Substrates: -
Products: -
Products: -
?
UTP + H2O + ketoconazole[side 1]
UDP + phosphate + ketoconazole[side 2]
Saccharomyces cerevisiae YRE1001
-
Substrates: -
Products: -
Products: -
?
UTP + H2O + rhodamine 6 G[side 1]
UDP + phosphate + rhodamine 6 G[side 2]
-
Substrates: -
Products: -
Products: -
?
UTP + H2O + rhodamine 6 G[side 1]
UDP + phosphate + rhodamine 6 G[side 2]
Saccharomyces cerevisiae YRE1001
-
Substrates: -
Products: -
Products: -
?
vinblastine/in + ATP + H2O
vinblastine/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
vinblastine/in + ATP + H2O
vinblastine/out + ADP + phosphate
-
Substrates: weak activity
Products: -
Products: -
?
vincristine/in + ATP + H2O
vincristine/out + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
vincristine/in + ATP + H2O
vincristine/out + ADP + phosphate
-
Substrates: -
Products: cotransport with reduced glutathione
Products: cotransport with reduced glutathione
?
vincristine/in + ATP + H2O
vincristine/out + ADP + phosphate
-
Substrates: requires cotransport of GSH
Products: -
Products: -
?
vincristine/in + ATP + H2O
vincristine/out + ADP + phosphate
-
Substrates: -
Products: -
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?
vincristine/in + ATP + H2O
vincristine/out + ADP + phosphate
-
Substrates: -
Products: -
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?
additional information
?
-
-
Substrates: transcription of the atrA and the atrB gene is strongly enhanced by treatment with several fungicides and plant defense toxins
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?
additional information
?
-
-
Substrates: BmrA is a half-ABC transporter involved in multidrug resistance
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?
additional information
?
-
-
Substrates: multidrug ABC transporter YvcC involved in multidrug resistance, the yvcC gene is constitutively expressed in Bacillus subtilis throughout its growth, the in vivo function is related to a protective role, the MDR pump might act as a housekeeping transporter to quickly cope with the presence of low levels of deleterious compounds, then, if the concentration of these compounds rose above a threshold limit, the expression of additional pumps could be turned on
Products: -
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?
additional information
?
-
-
Substrates: no hydrolysis of 5-adenylyl imidodiphosphate, study of YvcC interaction with different drugs
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?
additional information
?
-
-
Substrates: enzyme plays an important role in microbial resistance to neutral or positively charged amphiphilic drugs
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Products: -
?
additional information
?
-
-
Substrates: the recombinant enzyme in Saccharomyces cerevisiae is able to detoxify extracts of diverse plants collected in Mozambique, detailed overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant enzyme in Saccharomyces cerevisiae is able to detoxify extracts of diverse plants collected in Mozambique, detailed overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the P-glycoprotein contains two distinct sites for drug binding and transport, these sites interact in a positively cooperative manner
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Products: -
?
additional information
?
-
-
Substrates: the Pgp multidrug transporter carries out ATP-driven cellular efflux of a wide variety of hydrophobic drugs, natural products and peptides
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Products: -
?
additional information
?
-
-
Substrates: multidrug transporter, ATP-driven drug transport, the intimate association of both Pgp and its substrates with the membrane suggests that its function may be regulated by the biophysical properties of the lipid bilayer
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform Abcb5 does not transport the fluorescent P-gp probes BODIPY-ethylenediamine or LDS 751
Products: -
Products: -
?
additional information
?
-
-
Substrates: the fly enzyme exhibits a unique high level basal ATPase activity that is inhibited by the transported substrates, and it is capable of transporting several human MRP substrates like beta-estradiol 17-beta-D-glucuronide, leukotriene C4, calcein, fluo3 and carboxydichlorofluorescein
Products: -
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?
additional information
?
-
-
Substrates: enzyme plays an important role in microbial resistance to neutral or positively charged amphiphilic drugs
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?
additional information
?
-
-
Substrates: the enzyme could cleave phosphoester bonds effectively from a broad range of substrates such as ATP, AMP, p-nitrophenylphosphate and beta-glycerophosphate
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Products: -
?
additional information
?
-
-
Substrates: the enzyme operates in an alternating sites mechanism, that is when one catalytic site enters the transition state, the other is unable to do so
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?
additional information
?
-
-
Substrates: energy-dependent drug efflux pump
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?
additional information
?
-
-
Substrates: MRP3 is competent in the transport of glutathione S-conjugates, glucuronides and methotrexate, the enzyme is active in the transport of monoanionic human bile constituent glycocholate
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?
additional information
?
-
-
Substrates: enzyme confers cellular resistance to a variety of natural product cytotoxic agents
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?
additional information
?
-
-
Substrates: the deficient expression of cMRP appears as the basis of the transport defect in human Dubin-Johnson syndrome
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?
additional information
?
-
-
Substrates: potential protective role for the enzyme in chemical carcinogenesis
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?
additional information
?
-
-
Substrates: the physiological function can range from a protective role in chemical toxicity and oxidative stress to mediation of inflammatory responses involving cysteinyl leukotrienes
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?
additional information
?
-
-
Substrates: MRP5 might play a role in some cases of unexplained resistance to thiopurines in acute lymphoblastic leukemia and/or antiretroviral nucleoside analogs in HIV-infected patients
Products: -
Products: -
?
additional information
?
-
-
Substrates: MRP1 is an efflux pump, which can transport conjugated organic anions and cotansport vincristine together with GSH
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?
additional information
?
-
-
Substrates: exports a diverse group of natural products chemotherapeutic drugs, and hydrophobic peptides across the plasma membrane
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?
additional information
?
-
-
Substrates: overexpression of the multidrug resistance P-glycoprotein and the multidrug resistance-associated protein MRP1 is a principal cause of resistance of cancer to chemotherapy
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Products: -
?
additional information
?
-
-
Substrates: MRP1 is a key multidrug resistance ABC transporter in tumor cells
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?
additional information
?
-
-
Substrates: the ABC transporter P-glycoprotein is responsible for multidrug resistance in tumor cells
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?
additional information
?
-
-
Substrates: the ABC transporter MRP1 is involved in the cellular extrusion of conjugated metabolites and causes multidrug resistance in tumor cells
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?
additional information
?
-
-
Substrates: Pgp transports drugs out of cells
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?
additional information
?
-
-
Substrates: benzbromarone and MK571 may be potential transported substrates for MRP3
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?
additional information
?
-
-
Substrates: ATPase activity associated with P-glycoprotein is characterized by three drug-dependent phases: basal without drug, drug-activated, and drug-inhibited, the basal ATPase activity is not a consequence of transport of an endogenous lipid or other substrate, but rather an intrinsic mechanistic property of enzyme
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?
additional information
?
-
-
Substrates: binding of drugs to Pgp is not compatible with a classical key-lock or one-pharmacophore model but can be well explained with a modular binding concept, where the energetically most relevant binding module seems to consist of two hydrogen bond acceptor groups
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?
additional information
?
-
-
Substrates: the drug substrate binding site of isoform MDR1/P-glycoprotein may best fit to drugs with a molecular mass of between 800 and 900 Da, and cholesterol may support the recognition of smaller drugs by adjusting the drug-binding site
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?
additional information
?
-
-
Substrates: stimulation of elimination via MRP2 may result in suboptimal chemotherapeutic drug concentrations, and stimulation of MRP2 activity in tumors may lead to increased efflux of chemotherapeutic drugs and thereby drug resistance
Products: -
Products: -
?
additional information
?
-
-
Substrates: MRP1 is a primary active transporter of conjugated metabolites and endogenous organic anions including leukotriene C4 and glutathione. Enzyme mutations can lead to diabetes mellitus
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Products: -
?
additional information
?
-
-
Substrates: the intrinsic multidrug resistance, MDR, of cholangiocellular and gallbladder carcinomas seems to be independent of MRP2 expression while the expression of MRP3 may contribute to the MDR phenotype
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Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview. Renal excretion is an important route of elimination for many MRP4 substrates. MRP4 has a putative pathophysiological function in signalling, and it protects the liver from accumulation of toxic bile acids during cholestasis by facilitating their efflux into blood for ultimate renal excretion
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?
additional information
?
-
-
Substrates: MRP5 plays a role in the ocular drug efflux and conferring ocular drug resistance
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?
additional information
?
-
-
Substrates: The polylactoseamine oligosaccharides on the first loop of P-gp 170 can specifically bind the tomato lectin which possibly stabilizes the functional active conformation of P-gp
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme molecular modeling, overview
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Products: -
?
additional information
?
-
-
Substrates: Tyr440, naturally occuring in wild-type MRP3 and recombinantly in MRP1 mutants, makes a major contribution to recognition of GSH and the GSH moiety of conjugates such as LTC4
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Products: -
?
additional information
?
-
-
Substrates: P-glycoprotein seems to prefer amphipathic cationic compounds, and MRP1 anionic compounds
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?
additional information
?
-
-
Substrates: Pgp transport studies across recombinant MDCK-MDR1 monolayers, overview
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Products: -
?
additional information
?
-
-
Substrates: MRP7 has a broad resistance profile for natural products, no transport activity with nontaxane antimicrotubule agents
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?
additional information
?
-
-
Substrates: ligand binding structure analysis using the three-dimensional structure modelling, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the human multidrug resistance transporter P-glycoprotein prevents the entry of compounds into the brain by an active efflux mechanism at the blood-brain barrier
Products: -
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?
additional information
?
-
-
Substrates: P-gp possesses a linker region of about 75 amino acids that connects two homologous halves, each of which contain a transmembrane domain followed by a nucleotide-binding domain. The linker region regulates the inherent substrate specificity of P-gp
Products: -
Products: -
?
additional information
?
-
Substrates: tested compounds exhibiting similar influx as efflux induce different ATPase activity profiles in cells and inside-out vesicles. Their concentration is significantly lower in the cytosolic leaflet of cells than in the cytosolic leaflet of inside-out membrane vesicles, indicating that P-glycoprotein can cope with passive influx. P-glycoprotein thus transports all compounds tested at a rate proportional to ATP hydrolysis. However, it prevents substrate entry into the cytosol only if passive influx of substrates across the lipid bilayer is in a similar range as active efflux
Products: -
Products: -
?
additional information
?
-
Substrates: n-dodecyl-beta-D-maltoside is no substrate for the enzyme, and the presence of n-dodecyl-beta-D-maltoside does not alter the locations of drug-binding sites, e.g. for tariquidar. The enzyme shows drug-stimulated ATPase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: n-dodecyl-beta-D-maltoside is no substrate for the enzyme, and the presence of n-dodecyl-beta-D-maltoside does not alter the locations of drug-binding sites, e.g. for tariquidar. The enzyme shows drug-stimulated ATPase activity
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not transport verapamil
Products: -
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?
additional information
?
-
-
Substrates: the enzyme possesses the ability for simultaneous drug binding
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?
additional information
?
-
Substrates: the enzyme does not transport arsenate
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?
additional information
?
-
-
Substrates: possible role for LmrA in lipid trafficking
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Products: -
?
additional information
?
-
Substrates: role of the YdaG/YdbA heterodimer in drug resistance
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Products: -
?
additional information
?
-
-
Substrates: role of the YdaG/YdbA heterodimer in drug resistance
Products: -
Products: -
?
additional information
?
-
-
Substrates: LmrA and the lipid transporter MsbA in Escherichia coli have overlapping specificities for Lipid A and chemotherapeutic and cytotoxic drugs
Products: -
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?
additional information
?
-
Substrates: role of the YdaG/YdbA heterodimer in drug resistance
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Products: -
?
additional information
?
-
-
Substrates: possible role for LmrA in lipid trafficking
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Products: -
?
additional information
?
-
-
Substrates: enzyme plays an important role in microbial resistance to neutral or positively charged amphiphilic drugs
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme functions as cotransporter of glutathione and natural product toxins
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Products: -
?
additional information
?
-
-
Substrates: energy-dependent drug efflux pump
Products: -
Products: -
?
additional information
?
-
-
Substrates: baseline enzyme expression protects cells from the toxic effects of xenobiotics by effluxing the xenobiotics and GSH from the intracellular compartment into the extracellular medium by a cotransport mechanism
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme in the canalicular membrane plays an important role in the excretion of phospholipid into bile
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant enzyme in Saccharomyces cerevisiae is able to detoxify extracts of diverse plants collected in Mozambique, detailed overview
Products: -
Products: -
?
additional information
?
-
Nakaseomyces glabratus CCM8270
-
Substrates: the recombinant enzyme in Saccharomyces cerevisiae is able to detoxify extracts of diverse plants collected in Mozambique, detailed overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MRP5 plays a role in the ocular drug efflux lowering the permeability of antiviral and glaucoma drugs and conferring ocular drug resistance
Products: -
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?
additional information
?
-
Substrates: the enzyme also possesses Na+/H+, K+/H, and Li+/H+ antiport activity
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?
additional information
?
-
Substrates: no activity with erythromycin, tetracycline or rifampicin
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?
additional information
?
-
Planococcus maritimus DS 17275T
Substrates: the enzyme also possesses Na+/H+, K+/H, and Li+/H+ antiport activity
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?
additional information
?
-
-
Substrates: enzyme plays an important role in microbial resistance to neutral or positively charged amphiphilic drugs
Products: -
Products: -
?
additional information
?
-
-
Substrates: Pgh1 is not involved as a chloroquine transporter in the plasma membrane of Plasmodium falciparum
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?
additional information
?
-
-
Substrates: substrate comparison between fish P-glycoprotein and human P-glycoprotein, identification of five compounds that specifically interact only with fish P-glycoprotein, while seven compounds exhibit specific interaction only with human P-glycoprotein. Sixteen tested compounds show interaction with both proteins, and there is significant correlation in the interaction potency between fish and human P-glycoprotein for those compounds that interact with both proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: no transport of endothelin I and Arg8-vasopressin by MRP6
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?
additional information
?
-
-
Substrates: phosphatidylinositol 3-kinase activity is necessary for maximal ATP-dependent transport of taurocholate and dinitrophenyl-glutathione in vivo. Type I phosphatidylinositol 3-kinase lipid products directly regulate ATP-dependent membrane transport system and function of ATP binding cassette membrane proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not play a major role in canalicular organic anion excretion. The enzyme might fulfill a housekeeping transport function involved in the regulation of paracellular and/or transcellular solute movement from blood into bile
Products: -
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?
additional information
?
-
-
Substrates: no transport of endothelin I and Arg8-vasopressin by MRP6
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not play a major role in canalicular organic anion excretion. The enzyme might fulfill a housekeeping transport function involved in the regulation of paracellular and/or transcellular solute movement from blood into bile
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not exhibit adenylate kinase activity
Products: -
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?
additional information
?
-
Saccharomyces cerevisiae YRE1001
-
Substrates: the enzyme does not exhibit adenylate kinase activity
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?
additional information
?
-
-
Substrates: adult worms from the Egyptian Schistosoma mansoni isolate with reduced sensitivity to praziquantel express increased levels of SMDR2
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?
additional information
?
-
-
Substrates: subunit DrrA of DrrAB hydrolyzes ATP, and the energy is transduced to carrier DrrB resulting in export of drugs
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Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + 17beta-estradiol 17-(beta-D-glucuronide)/in
ADP + phosphate + 17beta-estradiol 17-(beta-D-glucuronide)/out
ATP + H2O + 4-(2-aminoethyl)benzenesulfonylfluoride/in
ADP + phosphate + 4-(2-aminoethyl)benzenesulfonylfluoride/out
-
Substrates: -
Products: -
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?
ATP + H2O + 4-aminohippuric acid/in
ADP + phosphate + 4-aminohippuric acid/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 5-(glutathione-S-yl)-N-methyl-alpha-methyldopamine/in
ADP + phosphate + 5-(glutathione-S-yl)-N-methyl-alpha-methyldopamine/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + acyclovir/in
ADP + phosphate + acyclovir/out
-
Substrates: -
Products: -
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?
ATP + H2O + adefovir/in
ADP + phosphate + adefovir/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + allopurinol/in
ADP + phosphate + allopurinol/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + azole/in
ADP + phosphate + azole/out
-
Substrates: the ABC multidrug transporter Cdr1p plays a key role in azole resistance
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Products: -
?
ATP + H2O + beta-estradiol/in
ADP + phosphate + beta-estradiol/out
-
Substrates: -
Products: -
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?
ATP + H2O + bimatoprost/in
ADP + phosphate + bimatoprost/out
-
Substrates: -
Products: -
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?
ATP + H2O + calcein/in
ADP + phosphate + calcein/out
-
Substrates: fluorescent substrate of MRP1
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?
ATP + H2O + cefazolin/in
ADP + phosphate + cefazolin/out
-
Substrates: -
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?
ATP + H2O + cefmetazole/in
ADP + phosphate + cefmetazole/out
-
Substrates: -
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?
ATP + H2O + cefotaxime/in
ADP + phosphate + cefotaxime/out
-
Substrates: -
Products: -
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?
ATP + H2O + ceftizoxime/in
ADP + phosphate + ceftizoxime/out
-
Substrates: -
Products: -
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?
ATP + H2O + celecoxib/in
ADP + phosphate + celecoxib/out
-
Substrates: -
Products: -
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?
ATP + H2O + chenodeoxycholylglycine/in
ADP + phosphate + chenodeoxycholylglycine/out
-
Substrates: -
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?
ATP + H2O + chenodeoxycholyltaurine/in
ADP + phosphate + chenodeoxycholyltaurine/out
-
Substrates: -
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?
ATP + H2O + cholate/in
ADP + phosphate + cholate/out
-
Substrates: -
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?
ATP + H2O + cholesterol/in
ADP + phosphate + cholesterol/out
-
Substrates: P-gp may actively mediate cholesterol redistribution in the cell membrane, P-gp mediates the ATP-dependent relocation of cholesterol from the cytosolic leaflet to the exoplasmic leaflet of the plasma membrane, P-gp likely contributes in stabilizing the cholesterol-rich microdomains, rafts and caveolae, and is involved in the regulation of cholesterol trafficking in cells
Products: -
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?
ATP + H2O + cholesterol[side 1]
ADP + phosphate + cholesterol[side 2]
Substrates: the enzyme does not catalyze significant cholesterol transport in vivo
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?
ATP + H2O + cholylglycine/in
ADP + phosphate + cholylglycine/out
-
Substrates: -
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?
ATP + H2O + cholytaurine/in
ADP + phosphate + cholytaurine/out
-
Substrates: -
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?
ATP + H2O + corticosterone/in
ADP + phosphate + corticosterone/out
-
Substrates: -
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?
ATP + H2O + cyclosporine A[side 1]
ADP + phosphate + cyclosporine A [side 2]
Substrates: -
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?
ATP + H2O + daunorubicin/in
ADP + phosphate + daunorubicin/out
-
Substrates: fluorescent substrate of P-glycoprotein
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?
ATP + H2O + dehydroepiandrosterone sulfate/in
ADP + phosphate + dehydroepiandrosterone sulfate/out
-
Substrates: -
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?
ATP + H2O + deoxycholylglycine/in
ADP + phosphate + deoxycholylglycine/out
-
Substrates: -
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?
ATP + H2O + dipyridamole/in
ADP + phosphate + dipyridamole/out
-
Substrates: -
Products: -
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?
ATP + H2O + edaravone glucuronide/in
ADP + phosphate + edaravone glucuronide/out
-
Substrates: -
Products: -
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?
ATP + H2O + estrone-3-sulfate/in
ADP + phosphate + estrone-3-sulfate/out
-
Substrates: -
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?
ATP + H2O + ethidium[side 1]
ADP + phosphate + ethidium[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + fluconazole/in
ADP + phosphate + fluconazole/out
-
Substrates: -
Products: -
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?
ATP + H2O + furosemide/in
ADP + phosphate + furosemide/out
-
Substrates: -
Products: -
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?
ATP + H2O + GSH-conjugated 4-hydroxy-2-nonenal/in
ADP + phosphate + GSH-conjugated 4-hydroxy-2-nonenal/out
-
Substrates: -
Products: -
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?
ATP + H2O + GSH-conjugated prostaglandin A2/in
ADP + phosphate + GSH-conjugated prostaglandin A2/out
-
Substrates: -
Products: -
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?
ATP + H2O + guanidinium ion[side 1]
ADP + phosphate + guanidinium ion[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + hydrochlorothiazide/in
ADP + phosphate + hydrochlorothiazide/out
-
Substrates: -
Products: -
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?
ATP + H2O + indomethacin/in
ADP + phosphate + indomethacin/out
-
Substrates: -
Products: -
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?
ATP + H2O + latanoprost/in
ADP + phosphate + latanoprost/out
-
Substrates: -
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?
ATP + H2O + leucovorin/in
ADP + phosphate + leucovorin/out
-
Substrates: -
Products: -
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?
ATP + H2O + leukotriene B4/in
ADP + phosphate + leukotriene B4/out
-
Substrates: MRP4 only transports leukotriene B4 in the presence of glutathione
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?
ATP + H2O + leukotriene E4/in
ADP + phosphate + leukotriene E4/out
-
Substrates: -
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?
ATP + H2O + lysophosphatidylinositol/in
ADP + phosphate + lysophosphatidylinositol/out
-
Substrates: -
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?
ATP + H2O + MTS-rhodamine [side 1]
ADP + phosphate + MTS-rhodamine [side 2]
Substrates: the binding site in transmembrane segment 5 is F343C for rhodamine
Products: -
Products: -
?
ATP + H2O + olmesartan/in
ADP + phosphate + olmesartan/out
-
Substrates: -
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?
ATP + H2O + p-methoxy-ethylamphetamine/in
ADP + phosphate + p-methoxy-ethylamphetamine/out
ATP + H2O + paclitaxel/in
ADP + phosphate + paclitaxel/out
-
Substrates: -
Products: -
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?
ATP + H2O + phosphatidylcholine/in
ADP + phosphate + phosphatidylcholine/out
Substrates: -
Products: -
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?
ATP + H2O + probenecid/in
ADP + phosphate + probenecid/out
-
Substrates: -
Products: -
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?
ATP + H2O + prostaglandin A2/in
ADP + phosphate + prostaglandin A2/out
-
Substrates: -
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?
ATP + H2O + prostaglandin E1/in
ADP + phosphate + prostaglandin E1/out
-
Substrates: -
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?
ATP + H2O + prostaglandin E2/in
ADP + phosphate + prostaglandin E2/out
-
Substrates: -
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?
ATP + H2O + prostaglandin F2alpha/in
ADP + phosphate + prostaglandin F2alpha/out
-
Substrates: -
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?
ATP + H2O + rhodamine B[side 1]
ADP + phosphate + rhodamine B[side 2]
-
Substrates: -
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?
ATP + H2O + sphingosine-1-phosphate/in
ADP + phosphate + sphingosine-1-phosphate/out
-
Substrates: -
Products: -
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ATP + H2O + tariquidar [side 1]
ADP + phosphate + tariquidar [side 2]
Substrates: -
Products: -
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ATP + H2O + taurocholate/in
ADP + phosphate + taurocholate/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + tenofovir/in
ADP + phosphate + tenofovir/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + thromboxane B2/in
ADP + phosphate + thromboxane B2/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + topotecan/in
ADP + phosphate + topotecan/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + urate/in
ADP + phosphate + urate/out
-
Substrates: MRP4 is the first secretory transporter identified in the bidirectional renal handling of urate and could be a potential drug target in the treatment of hyperuricaemia, regulation, overview
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ATP + H2O + ursodeoxycholylglycine/in
ADP + phosphate + ursodeoxycholylglycine/out
-
Substrates: -
Products: -
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ATP + H2O + ursodeoxycholyltaurine/in
ADP + phosphate + ursodeoxycholyltaurine/out
-
Substrates: -
Products: -
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ATP + H2O + verapamil [side 1]
ADP + phosphate + verapamil [side 2]
Substrates: the binding site in transmembrane segment 5 is I306C for verapamil
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ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
Substrates: -
Products: -
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GTP + H2O + ethidium[side 1]
GDP + phosphate + ethidium[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + 17beta-estradiol 17-(beta-D-glucuronide)/in
ADP + phosphate + 17beta-estradiol 17-(beta-D-glucuronide)/out
-
Substrates: transported by MRP1 and MRP3
Products: -
Products: -
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ATP + H2O + 17beta-estradiol 17-(beta-D-glucuronide)/in
ADP + phosphate + 17beta-estradiol 17-(beta-D-glucuronide)/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin/in
ADP + phosphate + doxorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + doxorubicin/in
ADP + phosphate + doxorubicin/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: natural substrate of MRP1
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ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: -
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ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: glutathione is not required
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ATP + H2O + leukotriene C4/in
ADP + phosphate + leukotriene C4/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + methotrexate/in
ADP + phosphate + methotrexate/out
-
Substrates: -
Products: -
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?
ATP + H2O + methotrexate/in
ADP + phosphate + methotrexate/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + p-methoxy-ethylamphetamine/in
ADP + phosphate + p-methoxy-ethylamphetamine/out
-
Substrates: -
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ATP + H2O + p-methoxy-ethylamphetamine/in
ADP + phosphate + p-methoxy-ethylamphetamine/out
-
Substrates: cell resistance against the drug substrate is diminished by ATP depletion and enzyme inhibition
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Products: -
?
ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: the enzyme plays an important role in drug resistance
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ATP + H2O + rhodamine 123/in
ADP + phosphate + rhodamine 123/out
-
Substrates: -
Products: -
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?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: importance of Candida drug resistance protein Cdr1p of pathogenic Candida albicans in azole resistance
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
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?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: expression at the tumor cell surface of P-glycoprotein, which functions as an ATP-powered multidrug efflux pump, is involved in multidrug resistance. It also shows lipid flippase activity
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: multidrug resistance, the major physiological role is the protection of cells and tissues against xenobiotics, relevance of MRP1 and MRP3 proteins in chemoresistance of cancer and in drug metabolism and toxicity
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: MDR1, multiple drug resistance, ABC transporter, which acts as ATP-driven pump that removes xenobiotics from the interior of cells
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: ATP-driven pumping of a variety of drugs out of cells, multidrug resistance, hydrophobic model of drug transport by P-glycoprotein
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: P-glycoprotein is a membrane ATP-driven drug exporter, Pgp actively extrudes a spectrum of hydrophobic xenobiotics, including a number of anticancer drugs
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: MRP1 transports a wide range of natural product drugs and structurally diverse conjugated and unconjugated organic anions. Its closest relative is MRP3. MRP1 transports GSH and GSH conjugates and displays GSH-stimulated transport of a number of unconjugated and conjugated compounds. In contrast, MRP3 does not transport GSH and is a poor transporter of GSH conjugates
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: the P-glycoprotein mediates multidrug resistance, which can be overcome by enzyme inhibition and ATP depletion allowing drug containing nanoparticles to target both drug and biological mechanisms
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
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Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: multidrug resistance protein MDR1, i.e. P-glycoprotein or ABCB1, is an ATP-dependent efflux pump for various cytotoxic agents, and is implicated in the resistance of human tumors to chemotherapeutic drugs
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Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: MRP4 limits brain entry and promotes renal excretion of drugs. In addition to its role in the body distribution and renal excretion of a wide variety of antiviral, cytostatic, antibiotic and cardiovascular drugs, MRP4/ABCC4 has the ability to transport molecules involved in cellular signalling. These molecules include cyclic nucleotides, eicosanoids, urate and conjugated steroids. The unique structure, regulation and dual localisation of MRP4 in polarised cells could be connected with a key function in cellular protection and extracellular signalling pathways, overview
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: the enzyme increases the resistance level of cells against drugs, overview
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?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: P-gp 170 has two potentially interesting regions for drugs interfering with its efflux function, namely the oligosaccharides on the first extracellular loop with unknown function and the two intracellular ATP-binding regions providing the energy for drug efflux function. P-gp is a polytopic plasma membrane protein whose overexpression causes multidrug resistance, MDR, responsible for the failure of cancer chemotherapy
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: P-glycoprotein belongs to the family of ATP-binding cassette proteins which hydrolyze ATP to catalyse the translocation of their substrates through membranes
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: the ATP-binding cassette multidrug resistance protein 1 mediates ATP-dependent cellular efflux of drugs and organic anions
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: in the brain, MRP4 limits the entry of drugs and is involved in nociception, probably as a result of reduced plasma prostaglandins. In the kidney, MRP4 mediates the active tubular secretion of diuretics, antiviral nucleosides and cephalosporins. In the liver, MRP4 mediates the efflux of bile acid to the blood, and knockout mice are more sensitive to cholestatic-induced liver injury. MRP4 protects bone marrow cells and the gastrointestinal tract against cytotoxic drugs and appears to be involved in secretory diarrhoea via coupling with CFTR
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
Nakaseomyces glabratus CCM8270
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: SMDR2 is an ATP-dependent efflux pump involved in transport of toxins and xenobiotics from cells
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Products: -
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ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
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ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
Substrates: -
Products: -
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additional information
?
-
-
Substrates: transcription of the atrA and the atrB gene is strongly enhanced by treatment with several fungicides and plant defense toxins
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additional information
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-
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Substrates: BmrA is a half-ABC transporter involved in multidrug resistance
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additional information
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-
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Substrates: multidrug ABC transporter YvcC involved in multidrug resistance, the yvcC gene is constitutively expressed in Bacillus subtilis throughout its growth, the in vivo function is related to a protective role, the MDR pump might act as a housekeeping transporter to quickly cope with the presence of low levels of deleterious compounds, then, if the concentration of these compounds rose above a threshold limit, the expression of additional pumps could be turned on
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additional information
?
-
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Substrates: enzyme plays an important role in microbial resistance to neutral or positively charged amphiphilic drugs
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Products: -
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additional information
?
-
-
Substrates: the recombinant enzyme in Saccharomyces cerevisiae is able to detoxify extracts of diverse plants collected in Mozambique, detailed overview
Products: -
Products: -
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additional information
?
-
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Substrates: the recombinant enzyme in Saccharomyces cerevisiae is able to detoxify extracts of diverse plants collected in Mozambique, detailed overview
Products: -
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additional information
?
-
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Substrates: the Pgp multidrug transporter carries out ATP-driven cellular efflux of a wide variety of hydrophobic drugs, natural products and peptides
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additional information
?
-
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Substrates: multidrug transporter, ATP-driven drug transport, the intimate association of both Pgp and its substrates with the membrane suggests that its function may be regulated by the biophysical properties of the lipid bilayer
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additional information
?
-
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Substrates: enzyme plays an important role in microbial resistance to neutral or positively charged amphiphilic drugs
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additional information
?
-
-
Substrates: energy-dependent drug efflux pump
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additional information
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-
-
Substrates: MRP3 is competent in the transport of glutathione S-conjugates, glucuronides and methotrexate, the enzyme is active in the transport of monoanionic human bile constituent glycocholate
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additional information
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Substrates: enzyme confers cellular resistance to a variety of natural product cytotoxic agents
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additional information
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-
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Substrates: the deficient expression of cMRP appears as the basis of the transport defect in human Dubin-Johnson syndrome
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additional information
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Substrates: potential protective role for the enzyme in chemical carcinogenesis
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additional information
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-
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Substrates: the physiological function can range from a protective role in chemical toxicity and oxidative stress to mediation of inflammatory responses involving cysteinyl leukotrienes
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additional information
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Substrates: MRP5 might play a role in some cases of unexplained resistance to thiopurines in acute lymphoblastic leukemia and/or antiretroviral nucleoside analogs in HIV-infected patients
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additional information
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Substrates: MRP1 is an efflux pump, which can transport conjugated organic anions and cotansport vincristine together with GSH
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additional information
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Substrates: exports a diverse group of natural products chemotherapeutic drugs, and hydrophobic peptides across the plasma membrane
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additional information
?
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-
Substrates: overexpression of the multidrug resistance P-glycoprotein and the multidrug resistance-associated protein MRP1 is a principal cause of resistance of cancer to chemotherapy
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additional information
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Substrates: MRP1 is a key multidrug resistance ABC transporter in tumor cells
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additional information
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Substrates: the ABC transporter P-glycoprotein is responsible for multidrug resistance in tumor cells
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additional information
?
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Substrates: the ABC transporter MRP1 is involved in the cellular extrusion of conjugated metabolites and causes multidrug resistance in tumor cells
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additional information
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Substrates: Pgp transports drugs out of cells
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additional information
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Substrates: binding of drugs to Pgp is not compatible with a classical key-lock or one-pharmacophore model but can be well explained with a modular binding concept, where the energetically most relevant binding module seems to consist of two hydrogen bond acceptor groups
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additional information
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Substrates: the drug substrate binding site of isoform MDR1/P-glycoprotein may best fit to drugs with a molecular mass of between 800 and 900 Da, and cholesterol may support the recognition of smaller drugs by adjusting the drug-binding site
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additional information
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Substrates: stimulation of elimination via MRP2 may result in suboptimal chemotherapeutic drug concentrations, and stimulation of MRP2 activity in tumors may lead to increased efflux of chemotherapeutic drugs and thereby drug resistance
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additional information
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Substrates: MRP1 is a primary active transporter of conjugated metabolites and endogenous organic anions including leukotriene C4 and glutathione. Enzyme mutations can lead to diabetes mellitus
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additional information
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Substrates: the intrinsic multidrug resistance, MDR, of cholangiocellular and gallbladder carcinomas seems to be independent of MRP2 expression while the expression of MRP3 may contribute to the MDR phenotype
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additional information
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Substrates: substrate specificity, overview. Renal excretion is an important route of elimination for many MRP4 substrates. MRP4 has a putative pathophysiological function in signalling, and it protects the liver from accumulation of toxic bile acids during cholestasis by facilitating their efflux into blood for ultimate renal excretion
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additional information
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Substrates: MRP5 plays a role in the ocular drug efflux and conferring ocular drug resistance
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additional information
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Substrates: The polylactoseamine oligosaccharides on the first loop of P-gp 170 can specifically bind the tomato lectin which possibly stabilizes the functional active conformation of P-gp
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additional information
?
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Substrates: the human multidrug resistance transporter P-glycoprotein prevents the entry of compounds into the brain by an active efflux mechanism at the blood-brain barrier
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additional information
?
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Substrates: possible role for LmrA in lipid trafficking
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Products: -
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additional information
?
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Substrates: role of the YdaG/YdbA heterodimer in drug resistance
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additional information
?
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Substrates: role of the YdaG/YdbA heterodimer in drug resistance
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additional information
?
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Substrates: role of the YdaG/YdbA heterodimer in drug resistance
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additional information
?
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Substrates: possible role for LmrA in lipid trafficking
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additional information
?
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-
Substrates: enzyme plays an important role in microbial resistance to neutral or positively charged amphiphilic drugs
Products: -
Products: -
?
additional information
?
-
-
Substrates: energy-dependent drug efflux pump
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additional information
?
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Substrates: baseline enzyme expression protects cells from the toxic effects of xenobiotics by effluxing the xenobiotics and GSH from the intracellular compartment into the extracellular medium by a cotransport mechanism
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additional information
?
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Substrates: the enzyme in the canalicular membrane plays an important role in the excretion of phospholipid into bile
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additional information
?
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Substrates: the recombinant enzyme in Saccharomyces cerevisiae is able to detoxify extracts of diverse plants collected in Mozambique, detailed overview
Products: -
Products: -
?
additional information
?
-
Nakaseomyces glabratus CCM8270
-
Substrates: the recombinant enzyme in Saccharomyces cerevisiae is able to detoxify extracts of diverse plants collected in Mozambique, detailed overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MRP5 plays a role in the ocular drug efflux lowering the permeability of antiviral and glaucoma drugs and conferring ocular drug resistance
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additional information
?
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Substrates: enzyme plays an important role in microbial resistance to neutral or positively charged amphiphilic drugs
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additional information
?
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Substrates: Pgh1 is not involved as a chloroquine transporter in the plasma membrane of Plasmodium falciparum
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additional information
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Substrates: phosphatidylinositol 3-kinase activity is necessary for maximal ATP-dependent transport of taurocholate and dinitrophenyl-glutathione in vivo. Type I phosphatidylinositol 3-kinase lipid products directly regulate ATP-dependent membrane transport system and function of ATP binding cassette membrane proteins
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additional information
?
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Substrates: does not play a major role in canalicular organic anion excretion. The enzyme might fulfill a housekeeping transport function involved in the regulation of paracellular and/or transcellular solute movement from blood into bile
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additional information
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Substrates: does not play a major role in canalicular organic anion excretion. The enzyme might fulfill a housekeeping transport function involved in the regulation of paracellular and/or transcellular solute movement from blood into bile
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additional information
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Substrates: adult worms from the Egyptian Schistosoma mansoni isolate with reduced sensitivity to praziquantel express increased levels of SMDR2
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
binding and/or hydrolysis of ATP induce conformational changes that are transmitted from the nucleotide binding domains to the transmembrane domains
additional information
although ADP, rather than ATP, is bound, the nucleotide-binding domains in Sav1866 exhibit the conformation of the ATP-bound state
-
additional information
-
although ADP, rather than ATP, is bound, the nucleotide-binding domains in Sav1866 exhibit the conformation of the ATP-bound state
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
divalent cation required in the order of descending efficiency: Mg2+, Mn2+, Ca2+, Co2+
Co2+
-
divalent cation required in the order of descending efficiency: Mg2+, Mn2+, Ca2+, Co2+
Mg2+
Mn2+
-
divalent cation required in the order of descending efficiency: Mg2+, Mn2+, Ca2+, Co2+
Mg2+
-
divalent cation required in the order of descending efficiency: Mg2+, Mn2+, Ca2+, Co2+
Mg2+
-
required, both Mg2+ coordination and nucleotide binding contribute to the formation of the active site, entry of Mg2+ into the active site causes the first large conformational change that brings Trp326 and Cys193 in close proximity to each other, besides Trp326, typical Glu238 in the Q-loop also participates in coordination of Mg2+ by the N-terminal nucleotide binding domain
Mg2+
Mg2+ that is required for ATP hydrolysis is superior to other candidates like Ca2+, Co2+, and Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(17beta)-N-([trans-4-[(6-amino-9H-purin-9-yl)methyl]cyclohexyl]methyl)-3-oxoandrost-4-ene-17-carboxamide
-
daunorubicin accumulation is 99% of the accumulation in presence of 0.01 mM progesterone
(17beta)-N-[(2E)-4-(6-amino-9H-purin-9-yl)but-2-en-1-yl]-3-oxoandrost-4-ene-17-carboxamide
-
daunorubicin accumulation is 72% of the accumulation in presence of 0.01 mM progesterone
(17beta)-N-[(2Z)-4-(6-amino-9H-purin-9-yl)but-2-en-1-yl]-3-oxoandrost-4-ene-17-carboxamide
-
daunorubicin accumulation is 86% of the accumulation in presence of 0.01 mM progesterone
(17beta)-N-[4-(6-amino-9H-purin-9-yl)but-2-yn-1-yl]-3-oxoandrost-4-ene-17-carboxamide
-
daunorubicin accumulation is 61% of the accumulation in presence of 0.01 mM progesterone
(17beta)-N-[4-(6-amino-9H-purin-9-yl)butyl]-3-oxoandrost-4-ene-17-carboxamide
-
daunorubicin accumulation is 78% of the accumulation in presence of 0.01 mM progesterone
(17beta)-N-[4-[(6-amino-9H-purin-9-yl)methyl]benzyl]-3-oxoandrost-4-ene-17-carboxamide
-
daunorubicin accumulation is 98% of the accumulation in presence of 0.01 mM progesterone
(17beta)-N-[6-(6-amino-9H-purin-9-yl)hexyl]-3-oxoandrost-4-ene-17-carboxamide
-
daunorubicin accumulation is 111% of the accumulation in presence of 0.01 mM progesterone
(1beta,1'beta)-5-bromo-6,6',7,12-tetramethoxy-2-methylberbaman
-
is an effectively and potential agent in reversing Pgp-mediated multidrug resistance by inhibiting the transport function and expression of Pgp
(1E)-1,5-bis[3,5-bis(methoxymethoxy)phenyl]-4,4-dibromopent-1-en-3-one
58.7% inhibition at 0.01 mM
(1E)-1,5-bis[3,5-bis(methoxymethoxy)phenyl]-4,4-dichloropent-1-en-3-one
51.5% inhibition at 0.01 mM
(1E)-1,5-bis[3,5-bis(methoxymethoxy)phenyl]-4,4-difluoropent-1-en-3-one
44.4% inhibition at 0.01 mM
(1E)-1-[3,5-bis(methoxymethoxy)phenyl]-4,4-dimethylpent-1-en-3-one
14.9% inhibition at 0.01 mM
(1E,4E)-1,5-bis(4-hydroxy-3-methoxyphenyl)penta-1,4-dien-3-one
51.8% inhibition at 0.01 mM
(1E,4E)-1,5-bis[3,4-bis(methoxymethoxy)phenyl]penta-1,4-dien-3-one
84.3% inhibition at 0.01 mM
(1E,4E)-1-(2H-1,3-benzodioxol-5-yl)-5-[3,5-bis(methoxymethoxy)phenyl]penta-1,4-dien-3-one
57.4% inhibition at 0.01 mM
(1E,4E)-1-(4-hydroxy-3,5-dimethoxyphenyl)-5-(3,4,5-trimethoxyphenyl)penta-1,4-dien-3-one
82.9% inhibition at 0.01 mM
(1Z,4E)-1,5-bis[3,5-bis(methoxymethoxy)phenyl]-2-chloropenta-1,4-dien-3-one
83.2% inhibition at 0.01 mM
(1Z,4E)-5-[3,5-bis(methoxymethoxy)phenyl]-2-bromo-1-[2-bromo-3,5-bis(methoxymethoxy)phenyl]penta-1,4-dien-3-one
77.4% inhibition at 0.01 mM
(2aR,6aR,12bS,14bS)-10,17-dimethoxy-3,3,6,6-tetramethyl-2a,3,6a,7,12b,14b-hexahydro-2H,6H-chromeno[3,4-c]chromeno[4',3':4,5]pyrano[3,2-h]chromene-13,14-dione
-
inhibits Pgp- and MDR1-mediated daunorubicin transport in NIH-3T3 MDR1 cells
(2aR,6aS,12bR,14bS)-10,17-dimethoxy-3,3,6,6-tetramethyl-2a,3,6a,7,12b,14b-hexahydro-2H,6H-chromeno[3,4-c]chromeno[4',3':4,5]pyrano[3,2-h]chromene-13,14-dione
-
inhibits Pgp- and MDR1-mediated daunorubicin transport in NIH-3T3 MDR1 cells
(2E)-3-[3,5-bis(methoxymethoxy)phenyl]-N-methylprop-2-enamide
6.1% inhibition at 0.01 mM
(2E)-3-[3,5-bis(methoxymethoxy)phenyl]prop-2-enal
9.2% inhibition at 0.01 mM
(2E)-3-[3,5-bis(methoxymethoxy)phenyl]prop-2-enoic acid
0.3% inhibition at 0.01 mM
(2E,4E)-8-methyl-2,4-bis[(pyridin-3-yl)methylidene]-8-azabicyclo[3.2.1]octan-3-one
-
-
(2E,4E)-8-methyl-2,4-bis[(pyridin-4-yl)methylidene]-8-azabicyclo[3.2.1]octan-3-one
-
-
(2E,6E)-2,6-bis[(2-fluorophenyl)methylidene]cyclohexan-1-one
30.5% inhibition at 0.01 mM
(2E,6E)-2,6-bis[[3,5-bis(methoxymethoxy)phenyl]methylidene]cyclohexan-1-one
69.8% inhibition at 0.01 mM
(2R,4aR,7bR,9R,11aR,14bR)-2,5,5,9,12,12-hexamethyl-1,3,4,4a,5,8,9,10,11,11a,12,14b-dodecahydrobenzo[c]isochromeno[3,4-g]chromene-7,14(2H,7bH)-dione
-
inhibits Pgp- and MDR1-mediated daunorubicin transport in NIH-3T3 MDR1 cells
(3E,5E)-1-methyl-3,5-bis[(1-methyl-1H-imidazol-2-yl)methylidene]piperidin-4-one
-
-
(3E,5E)-1-methyl-3,5-bis[(3,4,5-trimethoxyphenyl)methylidene]piperidin-4-one
-
-
(3E,5E)-3,5-bis[(2-fluoro-4,5-dimethoxyphenyl)methylidene]-1-methylpiperidin-4-one
-
-
(3E,5E)-3,5-bis[[3,5-bis(methoxymethoxy)phenyl]methylidene]-1-methylpiperidin-4-one
52% inhibition at 0.01 mM
(4E)-5-[3,5-bis(methoxymethoxy)phenyl]-2-[[3,4-bis(methoxymethoxy)phenyl]methyl]-3-oxopent-4-enenitrile
29.9% inhibition at 0.01 mM
(6aS,9bR,15aS,18bR)-2,4,11,13-tetrabromo-7,7,16,16-tetramethyl-6a,15a,16,18b-tetrahydro-6H,15H-chromeno[3,4-c]chromeno[4',3':4,5]pyrano[2,3-g]chromene-9,18(7H,9bH)-dione
-
inhibits Pgp- and MDR1-mediated daunorubicin transport in NIH-3T3 MDR1 cells
(6aS,9bR,15aS,18bR)-3,12-dimethoxy-7,7,16,16-tetramethyl-6a,15a,16,18b-tetrahydro-6H,15H-chromeno[3,4-c]chromeno[4',3':4,5]pyrano[2,3-g]chromene-9,18(7H,9bH)-dione
-
inhibits Pgp- and MDR1-mediated daunorubicin transport in NIH-3T3 MDR1 cells
(R)-4-[(1a,6,10b)-1,1-dichloro-1,1a,6,10b-tetrahydrodibenzo[a,e]cyclopropa[c]cyclohepten-6-yl]-[(5-quinolinyloxy)methyl]-1-piperazineethanol
-
complete inhibition of P-glycoprotein at 0.005 mM
(R)-4-[(1a,6,10b)-1,1-difluoro-1,1a,6,10btetrahydrodibenzo[a,e]cyclopropa[c]cyclohepten-6-yl]-[(5-quin-olinyloxy)methyl]-1-piperazineethanol
-
LSN 335979, P-glycoprotein-specific inhibitor
1,13-bis[4'-(4H-chromen-4-on-2-yl)phenyl]-N-(benzyl)-1,4,10,13-tetraoxa-7-azatridecane
-
competitive inhibitor to doxorubicin binding by P-glycoprotein
1,5-bis[3,4-bis(methoxymethoxy)phenyl]-1,5-bis(phenylsulfanyl)pentan-3-one
26.6% inhibition at 0.01 mM
1,5-bis[3,4-bis(methoxymethoxy)phenyl]-1,5-bis[(2,3-dihydroxypropyl)sulfanyl]pentan-3-one
1.6% inhibition at 0.01 mM
1,5-bis[3,5-bis(methoxymethoxy)phenyl]-1,5-bis(ethylsulfanyl)pentan-3-one
37.1% inhibition at 0.01 mM
1-(4-acetylpiperazin-1-yl)-4-propoxy-9H-thioxanthen-9-one
-
uncompetitive, approximately 1.5fold more potent than verapamil in decreasing the doxorubicin GI50 on K-562 Dox cell line
1-isatin-4-(40-methoxyphenyl)-3-thiosemicarbazone
-
IC50 against KB-3-1 cells 0.0142 mM, against KB-VI cells 0.0033 mM. Displays MDR1-selectivity against all P-glycoprotein expressing cell lines examined, and cross-resistance is no observed. Selectivity is reversed by inhibitors of P-glycoprotein ATPase activity. Compound also shows selectivity for cells expressing mouse and hamster MDR1
1-isatin-4-(40-nitrophenyl)-3-thiosemicarbazone
-
IC50 against KB-3-1 cells 0.0171 mM, against KB-VI cells 0.0021 mM
1-isatin-4-(40-tert-butyl phenyl)-3-thiosemicarbazone
-
IC50 against KB-3-1 cells 0.0159 mM, against KB-VI cells 0.0148 mM
1-[[2-(4-nitrophenyl)ethyl]amino]-4-propoxy-9H-thioxanthen-9-one
-
uncompetitive, approximately 1.5fold more potent than verapamil in decreasing the doxorubicin GI50 on K-562 Dox cell line
16alpha-17beta-estradiol 17-(beta-D-glucuronide)
-
transport of aflatoxin B1-epoxide-GSH conjugate
17beta-estradiol 16-(beta-D-glucuronide)
-
transport of aflatoxin B1-epoxide-GSH conjugate
17beta-estradiol 3-sulfato-17-(beta-D-glucuronide)
-
transport of aflatoxin B1-epoxide-GSH conjugate
2'-(4-ethoxyphenyl)-5-(4-methylpiperazin-1-yl)-1H,1'H-2,5'-bibenzo[d]imidazole
-
almost complete inhibition of fish P-glycoprotein specific ATPase in micromolar concentrations
2,6-bis(4-(dimethylamino)phenyl)-4-(5-(piperidine-1-carbonothioyl)thien-2-yl)thiopyrylium chloride
-
81% inhibition of MRP1 at 0.01 mM
2,6-bis(4-(dimethylamino)phenyl)-4-(5-(piperidine-1-carbonyl)thien-2-yl)thiopyrylium hexafluorophosphate
-
78% inhibition of MRP1 at 0.01 mM
2,6-di-tert-butyl-4-(5-(piperidine-1-carbonothioyl)thien-2-yl)thiopyrylium hexafluorophosphate
-
11% inhibition of MRP1 at 0.01 mM
2,6-di-tert-butyl-4-(5-(piperidine-1-carbonothioyl)thiophen-2-yl)thiopyrylium chloride
-
32% inhibition of MRP1 at 0.01 mM
2-tert-butyl-6-(4-(dimethylamino)phenyl)-4-(5-(piperidine-1-carbonothioyl)thiophen-2-yl)thiopyrylium chloride
-
93% inhibition of MRP1 at 0.01 mM
2-tert-butyl-6-(4-(dimethylamino)phenyl)-4-(5-(piperidine-1-carbonyl)thien-2-yl)thiopyrylium hexafluorophosphate
-
59% inhibition of MRP1 at 0.01 mM
2-[4-(3-ethoxy-1-propenyl)phenyl]-4,5-bis-[4-(2-propylamino)phenyl]-1H-imidazole
-
i.e. OC144-093. Coadministration of OC144-093 with docetaxel enhances the oral bioavailability of docetaxel to a limited extent (8-26%) in humans, and has a good safety profile as well
3,6-bis(dimethylamino)-9-(4-dimethylaminophenyl)-thioxanthylium hexafluorophosphate
-
competitive inhibition of verapamil-dependent ATPase-activity
3,6-bis(dimethylamino)-9-phenyl-selenoxanthylium bromide
-
i.e. selenium-derivative of tetramethylrosamine, competitive inhibition of verapamil-dependent ATPase-activity
3-[(3-[[(1,3-dioxo-8-phenyl-3,3a,3b,8,8a,8b-hexahydroindeno[1',2':3,4]cyclobuta[1,2-c]pyrrol-2(1H)-yl)acetyl]oxy]propyl)(methyl)amino]propyl (2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoate
-
-
3-[(3-[[(2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoyl]oxy]propyl)amino]propyl (2E)-3-(anthracen-9-yl)prop-2-enoate
-
-
3-[(3-[[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]oxy]propyl)(methyl)amino]propyl 10-chloroanthracene-9-carboxylate
-
-
3-[(3-[[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]oxy]propyl)(methyl)amino]propyl 3,4,5-trimethoxybenzoate
-
-
3-[(3-[[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]oxy]propyl)(methyl)amino]propyl anthracene-9-carboxylate
-
-
3-[(3-[[3-(1,3-dioxo-8-phenyl-3,3a,3b,8,8a,8b-hexahydroindeno[1',2':3,4]cyclobuta[1,2-c]pyrrol-2(1H)-yl)propanoyl]oxy]propyl)(methyl)amino]propyl (2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoate
-
-
3-[(3-[[3-(6,7-dimethoxy-3,4-dihydroisoquinolin-2(1H)-yl)propanoyl]oxy]propyl)(methyl)amino]propyl (2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoate
-
-
3-[(3-[[bis(4-methoxyphenyl)acetyl]oxy]propyl)(methyl)amino]propyl (2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoate
-
-
3-[methyl(3-[[(2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoyl]oxy]propyl)amino]propyl (2E)-3-(3,4-dimethoxyphenyl)prop-2-enoate
-
-
3-[methyl(3-[[(2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoyl]oxy]propyl)amino]propyl (2E)-3-(anthracen-9-yl)prop-2-enoate
-
-
3-[methyl(3-[[(2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoyl]oxy]propyl)amino]propyl (2E)-3-(biphenyl-4-yl)prop-2-enoate
-
-
3-[methyl(3-[[(2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoyl]oxy]propyl)amino]propyl 3,3-diphenylprop-2-enoate
-
-
3-[methyl(3-[[(2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoyl]oxy]propyl)amino]propyl 3,4,5-trimethoxybenzoate
-
-
3-[methyl(3-[[(2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoyl]oxy]propyl)amino]propyl anthracene-9-carboxylate
-
-
3-[methyl(3-[[(2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoyl]oxy]propyl)amino]propyl biphenyl-4-carboxylate
-
-
3-[[3-[(diphenylacetyl)oxy]propyl](methyl)amino]propyl (2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoate
-
-
4-[5-(4-chlorophenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
i.e. SC236. The direct inhibitory effects of indomethacin and SC236 on P-gp may contribute to their ability to increase the intracellular retention of doxorubicin and thus enhance its cytotoxicity
5'-O-[4-(fluorosulfonyl)benzoyl]adenosine
-
incubation inhibits ATP hydrolysis and the binding of 8-azido-ATP. 5'-Fluorosulfonylbenzoyl 5'-adenosine is an ATP analog that interacts with both the drug-binding and ATP-binding sites of P-gp, but fluorosulfonyl-mediated crosslinking is observed only at the nucleotide-binding domains
5-[(5-[[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]oxy]pentyl)(methyl)amino]pentyl 3,4,5-trimethoxybenzoate
-
-
5-[(5-[[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]oxy]pentyl)(methyl)amino]pentyl anthracene-9-carboxylate
-
-
5-[(5-[[bis(4-methoxyphenyl)acetyl]oxy]pentyl)(methyl)amino]pentyl (2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoate
-
-
5-[methyl(5-[[(2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoyl]oxy]pentyl)amino]pentyl (2E)-3-(biphenyl-4-yl)prop-2-enoate
-
-
5-[methyl(5-[[(2E)-3-(3,4,5-trimethoxyphenyl)prop-2-enoyl]oxy]pentyl)amino]pentyl 3,3-diphenylprop-2-enoate
-
-
9,10-dihydro-5-methoxy-9-oxo-N-{4-[2-(1,2,3,4-tetrahydro-6,7-dimethoxy-2-isoquinolinyl)ethyl]phenyl}-4-acridine
-
i.e. GF120918. A good and safe P-gp inhibitor alternative for cyclosporin A in enhancing the oral bioavailability of paclitaxel
alpha-mangostin
effectively and selectively inhibits enzyme-mediated drug transport and reverses multidrug resistance in ABCG2-overexpressing cancer cells
ATPgammaS
-
existence of two binding sites for ATPS with remarkably different binding affinities. One site binds ATPgammaS with Kd of 6 microM and the second binds ATPgammaS with Kd of 0.74 mM
auraptene
-
stimulates the ATPase activity of MRP1. No inhibition of MRP1-mediated efflux by auraptene, but auraptene increases the accumulation of daunorubicin in KB-C2 cells
azido-ATP
-
competitive, binding activity of wild-type and mutant enzymes, overview
beta-sitosterol-O-glucoside
-
inhibits the efflux of the P-gp substrate rhodamine 123 in a concentration-dependent manner. Good candidates for the development of novel P-gp/MDR1 reversal agents which may enhance the accumulation and efficacy of chemotherapy agents
bis[(4aS,6R,8aS)-3-methoxy-11-methyl-5,6,9,10,11,12-hexahydro-4aH-[1]benzofuro[3a,3,2-ef][2]benzazepin-6-yl] decanedioate
-
galactamine dimer. the inhibitory activity of the inhibitor on P-gp transport of substrate is evaluated in cells that over-express P-gp
buprenorphine
-
inhibits paclitaxel transport, placental brush border membrane vesicles
byakangelicol
-
shows strong P-gp inhibition from the screening of P-gp inhibitor evaluated by quinidine permeation through the Caco-2 monolayer
carnosic acid
-
increases the accumulation of daunorubicin or rhodamine 123 in KB-C2 cells. The ATPase activity of P-glycoprotein is stimulated
carnosol
-
increases the accumulation of daunorubicin or rhodamine 123 in KB-C2 cells. The ATPase activity of P-glycoprotein is stimulated
cis-(Z)-flupentixol
-
is a non-competitive inhibitor that interacts with the substrate site but is not transported
D-alpha-tocopheryl polyethylene glycol 1000 succinate
-
i.e. TPGS 1000, water-soluble Vitamin E derivative. Inhibits substrate-induced ATPase activity without inducing significant ATPase activity on its own. Modulation of ATPase activity correlates with inhibitory potential for P-glycoprotein-mediated efflux
-
deacetylnomilin
-
inhibits the efflux of the P-gp substrate rhodamine 123 in a concentration-dependent manner. Good candidates for the development of novel P-gp/MDR1 reversal agents which may enhance the accumulation and efficacy of chemotherapy agents. Good candidates for the development of novel P-gp/MDR1 reversal agents which may enhance the accumulation and efficacy of chemotherapy agents
DEAE-D40
40 kDa diethylaminoethyl-dextran; 40 kDa diethylaminoethyl-dextran; 40 kDa diethylaminoethyl-dextran, significant inhibition of the enzyme
-
desloratadine
-
weakly inhibits daunorubicin transport, 19% of the inhibition caused by vanadate, IC50: 0.043 nM, desloratadine is no significant inhibitor of P-gp and should not cause clinical drug interactions with agents that are P-gp substrates
dodecyloctaglycol
-
uncompetitive inhibition of verapamil-induced Pgp ATPase activity
estradiol 17beta-D-glucuronide
-
competitive inhibition of the transport activity of Mdr2
flurazepam
-
inhibits daunorubicin efflux up to 80%, partially inhibits ATPase activity
gomisin A
-
strongly inhibits P-glycoprotein ATPase activity in cells overexpressing the enzyme. Alters substrate interaction of P-glycoprotein but itself is neither a substrate nor a competitive inhibitor
HEPES
-
uptake of P-glycoprotein substrates is substantially diminished when the HEPES concentration is raised to 25 mM. Addition of 15 or 25 mM HEPES in the uptake buffer results in significant reduction in the accumulation of P-glycoprotein substrates cyclosporine-A, ritonavir, and lopinavir. Bidirectional A-B and B-A transport studies show that permeability ratio in the presence of 25 mM HEPES is significantly higher than control. HEPES stimulates the production of ATP and modulates the energy dependent efflux and uptake processes
hesperidin
-
inhibits the efflux of the P-gp substrate rhodamine 123 in a concentration-dependent manner. Good candidates for the development of novel P-gp/MDR1 reversal agents which may enhance the accumulation and efficacy of chemotherapy agents
limonin
-
inhibits the efflux of the P-gp substrate rhodamine 123 in a concentration-dependent manner. Good candidates for the development of novel P-gp/MDR1 reversal agents which may enhance the accumulation and efficacy of chemotherapy agents
loratadine
-
inhibits daunorubicin transport, IC50: 0.011 nM, much less inhibitory than cyclosporin A or verapamil, 43% of the inhibition caused by vanadate
lovastatin
-
increases the absorption of verapamil (used as an antiarrhythmic agent to control supraventricular tachyarrhythmias) by inhibiting P-glycoprotein
methadone
-
inhibits paclitaxel transport, placental brush border membrane vesicles
methoxypolyethylene17 glycol-beta-caprolactone5
-
amphiphilic diblock copolymer, decreases membrane fluidity and inhibits enzyme-mediated efflux while stimulating the enzyme's ATPase activity up to 3fold
methyl (2E)-3-[3,5-bis(methoxymethoxy)phenyl]prop-2-enoate
8.6% inhibition at 0.01 mM
methylparathion
-
0.05 mM, stimulates ATPase activity by 30% and inhibits at higher concentrations
N,N'-[[1,5-bis[3,4-bis(methoxymethoxy)phenyl]-3-oxopentane-1,5-diyl]bis(sulfanediylethane-2,1-diyl)]diacetamide
15.2% inhibition at 0.01 mM
N-(2'-deoxy-beta-D-ribofuranosyl)-5-cyclohexyl-1H-indole
-
nontransported substrate of P-glycoprotein
N-(4-[2-(1,2,3,4-tetrahydro-6,7-dimethoxy-2-isoquinolinyl)ethyl]-phenyl)-9,10-dihydro-5-methoxy-9-oxo-4-acridine carboxamide
-
-
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]thiochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
competitive inhibition of verapamil-dependent ATPase-activity
N-[5-[1-(4-[2-[6-methoxy-7-[2-[2-(2-methoxyethoxy)ethoxy]ethoxy]-3,4-dihydroisoquinolin-2(1H)-yl]ethyl]phenyl)-1H-1,2,3-triazol-4-yl]-2-propanoylphenyl]quinoline-2-carboxamide
-
N-[6-(dimethylamino)-9-[5-(piperidin-1-ylcarbonyl)thiophen-2-yl]-3H-selenoxanthen-3-ylidene]-N-methylmethanaminium hexafluorophosphate
-
-
N-[6-(dimethylamino)-9-[5-(piperidin-1-ylcarbonyl)thiophen-2-yl]-3H-telluroxanthen-3-ylidene]-N-methylmethanaminium hexafluorophosphate
-
-
N-[6-(dimethylamino)-9-[5-(piperidin-1-ylcarbonyl)thiophen-2-yl]-3H-thioxanthen-3-ylidene]-N-methylmethanaminium hexafluorophosphate
-
-
N-[9-[3-(dimethylamino)phenyl]-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene]-N-methylmethanaminium bromide
-
-
N-[9-[4-(dimethylamino)phenyl]-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene]-N-methylmethanaminium bromide
-
-
nanoparticles
-
doxorubicin and paclitaxel nanoparticles inhibit P-glycoprotein and transiently deplete ATP, while cyclosporine A and polystyrene nanoparticles do not, overview
-
naringin
-
i.e. 7-[[2-O-(6-deoxy-alpha-L-mannopyra nosyl)-beta-D-glucopyranosyl]oxy]-2,3-dihydro-5-hydroxy-2-(4-hydroxyphenyl)-4H-1-benzo pyran-4-one. Pre-treatment with naringin prior to doxorubicin treatment increases the sensitivity of the enzyme to doxorubicin, naringin inhibits the doxorubicin-stimulated ATPase activity and may interact directly with the transporter. Naringin seems to modulate the in vivo expression of P-gp
neohesperidin
-
inhibits the efflux of the P-gp substrate rhodamine 123 in a concentration-dependent manner. Good candidates for the development of novel P-gp/MDR1 reversal agents which may enhance the accumulation and efficacy of chemotherapy agents
nobiletin
-
a chemopreventive citrus phytochemical from orange, stimulates the ATPase activity of MRP1. Nobiletin also increases the accumulation of calcein, a fluorescent substrate of MRP1, in KB/MRP cells, and of P-glycoprotein substrate daunorubicin in KB-C2 cells
procyanidin
-
markedly increases the accumulation of rhodamine 123 by inhibiting its efflux in a dose-dependent manner. A 5-fold increase in cellular Rh123 is observed for procyanidine at 0.01 mM. Procyanidine is a potent inhibitor of P-glycoprotein on blood-brain barrier and can improve the therapeutic effects on cerebral tumors of some drugs which are difficult to accumulate in the brain
PSC 833
-
PgP inhibitors increase uptake of doxorubicin in tumor cells close to blood vessels, have little effect on drug uptake into tumor cells at intermediate distances, and might have a paradoxical effect to decrease doxorubicin uptake into distal tumor cells. This effect probably contributes to the limited success of PgP inhibitors in clinical trials
Q-D4
2-hydroxypropyl-trimethylammonium-dextran of 4 kDa; 2-hydroxypropyl-trimethylammonium-dextran of 4 kDa; 2-hydroxypropyl-trimethylammonium-dextran of 4 kDa
-
Q-D70
2-hydroxypropyl-trimethylammonium-dextran of 70 kDa; 2-hydroxypropyl-trimethylammonium-dextran of 70 kDa; 2-hydroxypropyl-trimethylammonium-dextran of 70 kDa
-
resveratrol disulfate
-
acts as a competitive inhibitor of BCRP-mediated methotrexate transport
rifampicin
inhibition of doxorubicin transport by rifampicin occurs by a competitive mechanism
rivulobirin A
-
shows strong P-gp inhibition from the screening of P-gp inhibitor evaluated by quinidine permeation through the Caco-2 monolayer
S-propyl (2E)-3-[3,5-bis(methoxymethoxy)phenyl]prop-2-enethioate
28.2% inhibition at 0.01 mM
salinomycin
-
treatment of the multidrug resistant cell lines with salinomycin restores a normal drug sensitivity of these cells
stigmasterol
-
inhibits the efflux of the P-gp substrate rhodamine 123 in a concentration-dependent manner. Good candidates for the development of novel P-gp/MDR1 reversal agents which may enhance the accumulation and efficacy of chemotherapy agents
tert-butyl (3E,5E)-3,5-bis[(2,5-dimethoxyphenyl)methylidene]-4-oxopiperidine-1-carboxylate
-
-
tert-butyl (4R)-4-(benzyloxy)-1-(tert-butoxycarbonyl)-L-prolyl-N6-[(benzyloxy)carbonyl]-L-lysinate
tert-butyl 3-[(3S,6S,12aS)-6-(2-methylpropyl)-1,4-dioxo-9-[(prop-2-en-1-yl)oxy]-1,2,3,4,6,7,12,12a-octahydropyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl]propanoate
-
tert-butyl 3-[(3S,6S,12aS)-9-(cyclopentyloxy)-6-(2-methylprop-1-en-1-yl)-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydropyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl]propanoate
i.e. MZ-29
-
tert-butyl 3-[(3S,6S,12aS)-9-(cyclopentyloxy)-6-(2-methylpropyl)-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydropyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl]propanoate
-
tert-butyl [(3S,6S,12aS)-9-methoxy-6-(2-methylpropyl)-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydropyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl]acetate
-
tert-butyl [4-[(3S,6S,12aS)-9-methoxy-6-(2-methylpropyl)-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydropyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl]butyl]carbamate
-
tetrahydrocurcumin
-
inhibitory to P-glycoprotein as well as to mitoxantrone resistance protein and multidrug resistance protein1. Inhibition of transport function with concomitant stimulation of ATPase activity
trans,trans-4,17(20)-pregnadiene-3,16-dione
-
i.e. Z-guggulsterone. In presence of guggulsterone, fluorescent substrates daunorubicin or rhodamine 123 accumulate in KB-C2 cells. Efflux of rhodamine 123 is inhibited and the accumulation of substrate calcein is increased. ATPase activities of both isoforms ABCB1 And ABCC1 are stimulated
Triton X-100
-
uncompetitive inhibition of verapamil-induced Pgp ATPase activity
ursolic acid
-
increases the accumulation of daunorubicin or rhodamine 123 in KB-C2 cells. The ATPase activity of P-glycoprotein is stimulated
vincristine
-
alone is a very poor inhibitor of transport of leukotriene C4, together with GSH acts as relatively potent competitive inhibitor
wogonin
-
impairs the function of P-glycoprotein and increases cellular content of etoposide in HL-60 cells. Wogonin may be used to reduce the excretion of anticancer agents via P-glycoprotein and to increase the pharmacological action in cancer cells. Wogonin may play a role in overcoming multidrug resistance
XR9576
-
is a non-competitive inhibitor that interacts with the substrate site but is not transported
[2-(1H-benzimidazol-2-yl)ethanamine]-4-propoxy-9H-thioxanthen-9-one
-
uncompetitive, causes an accumulation rate of rhodamine-123 similar to that caused by verapamil in the K-562 Dox resistant cell line, and a decrease in ATP consumption by P-gp. At 10 mM, 12.5fold decrease in the GI50 value of doxorubicin in the K-562 Dox resistant cell line, being 2fold more potent than verapamil
17-beta-estradiol 17-beta-(D-glucuronide)
-
transport of aflatoxin B1-epoxide-GSH conjugate
benzbromarone
-
50% inhibition of N-ethylmaleimide S-glutathione activated ATPase activity of MRP1 at 0.01 mM, 50% inhibition of E217betaG uptake by MRP1 at 0.005-0.008 mM, inhibits E217betaG uptake by MRP3 at 0.05 mM, but greatly stimulates this activity at 0.001-0.02 mM
beryllium fluoride
-
0.25 mM, 86% inhibition of ATPase, 89% inhibition of UTPase, and 50% inhibition of GTPase activity
cholesterol
-
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
cholesterol
-
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
clotrimazole
-
noncompetitive, inhibitor interacts with the transporter at a site distinct from the ATP-binding domains. Transport of clotrimazole by the enzyme continues at intracellular concentrations of clotrimazole that should eliminate all ATPase activity. GTPase and UTPase activites of the enzyme are rather resistant to clotrimazole
cyclosporin A
-
inhibits the transport of tetramethylrosamine in a concentration-dependent manner, 0.004 mM: almost complete inhibition, competes for tetramethylrosamine transport at the drug binding site
cyclosporin A
-
inhibits CD4 T cell P-glycoprotein activity in HIV-infected adults initiating treatment with nucleoside reverse transcriptase inhibitors
cyclosporin A
-
inhibits transport of dexamethasone, ritonavir and vinblastine
cyclosporine A
-
almost complete inhibition of fish P-glycoprotein specific ATPase in nanomolar concentrations
doxorubicin
-
cis-inhibition without trans-inhibition on MDR1-mediated vinblastine efflux of Xenopus laevis oocytes expressing human P-glycoprotein
ethidium
-
inhibits ATPase activity and GTPase activity of the enzyme
glibenclamide
-
mutation of residue Tyr2 in MRP1 cannot alter the sensitivity to glibenclamide
GSH
-
alone is a very poor inhibitor of transport of leukotriene C4, together with vincristine acts as relatively potent competitive inhibitor
Hoechst 33342
inhibition of doxorubicin transport by Hoechst 33342 occurs by a competitive mechanism
indomethacin
-
the direct inhibitory effects of indomethacin and SC236 on P-gp may contribute to their ability to increase the intracellular retention of doxorubicin and thus enhance its cytotoxicity
methyl-beta-cyclodextrin
-
over 85% inhibition of ATPase at 10 mM, about 55% inhibition of the lipid flippase at 10 mM
methyl-beta-cyclodextrin
-
inhibits ATPase activity of P-gp, 5-10 mM, total inhibition
MK571
-
50% inhibition of N-ethylmaleimide S-glutathione activated ATPase activity of MRP1 at 0.01 mM, but slightly activates this activity at 500-2000 nM, 100% inhibition of E217betaG uptake by MRP1 at 0.01-0.05 mM, but stimulates this activity at 500-1000 nM, inhibits E217betaG uptake by MRP3 at 0.05-0.1 mM, but stimulates this activity at 0.002-0.005 mM
monoclonal antibiodies
-
monoclonal antibodies QCRL-2, QCRL-3, and QCRL-4 recognize distinct, non-overlapping epitopes of the enzyme MRP. The ability to inhibit MRP-dependent transport results from direct interactions with the nucleotide-binding domains of the protein that do not prevent the binding of ATP
-
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
-
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
competitive inhibition of verapamil-dependent ATPase-activity
orthovanadate
-
rapid and complete inhibition in the presence of ATP and Co2+, very stable Pgp-ADP-Vi-Co2+ complex
orthovanadate
orthovanadate significantly inhibits the efflux and increases accumulation of ethidium bromide and norfloxacin
orthovanadate
-
non-covalent inhibitor of ABC ATPases catalyzing a photo-oxidative cleavage, characterization of three cleavage sites within MRP1, influence of nucleotides and transported substrates on the cleavage reaction, mechanism
orthovanadate
-
0.3 mM, 93% inhibition of ATPase, 66% inhibition of UTPase, and 45% inhibition of GTPase activity
progesterone
-
inhibition of ATPase-activity arising from co-expression of isoforms ABCG5 and ABCG8
PSC833
-
potent inhibitor in nanomolar concentrations, with some residual activity
quinidine
-
trans-inhibition on MDR1-mediated vinblastine and digoxin efflux of Xenopus laevis oocytes expressing human P-glycoprotein
reserpine
reserpine significantly inhibits the efflux and increases accumulation of ethidium bromide and norfloxacin
ritonavir
-
inhibition of intestinal P-glycoprotein by ritonavir causes increased darunavir absorption
tariquidar
the substrate inhibits P-gp ATPase activity in membranes, but stimulates ATPase activity when purified P-gp is assayed in the in the presence of n-dodecyl-beta-D-maltoside/sheep brain lipids. When wild-type human P-gp is expressed in Sf9 insect cells and the membranes are assayed for activity in the absence or presence of saturating concentrations of tariquidar, tariquidar reduces basal ATPase activity by about 60%
tert-butyl (4R)-4-(benzyloxy)-1-(tert-butoxycarbonyl)-L-prolyl-N6-[(benzyloxy)carbonyl]-L-lysinate
-
noncompetitive inhibitor towards daunorubicin and Hoechst 33342
tert-butyl (4R)-4-(benzyloxy)-1-(tert-butoxycarbonyl)-L-prolyl-N6-[(benzyloxy)carbonyl]-L-lysinate
-
noncompetitive inhibitor towards daunorubicin and Hoechst 33342
vanadate
-
ATPase activity is highly sensitive to vanadate inhibition, 0.01 mM: 50% inhibition
vanadate
-
inhibits Pgp ATPase and tetramethylrosamine transport activity, interacts with the nucleotide-binding domain
vanadate
-
0.01 mM, the basal and fenvalerate or verapamil-stimulated ATPase activities are inhibited
vanadate
complete inhibition of doxorubicin transport at 0.1 mM vanadate
verapamil
-
inhibits the transport of tetramethylrosamine in a concentration-dependent manner, 0.02 mM: almost complete inhibition, competes for tetramethylrosamine transport at the drug binding site
verapamil
-
the substrate is one of the most potent activators of P-gp ATPase activity, but inhibits calcein uptake
verapamil
-
trans-inhibition on MDR1-mediated vinblastine and digoxin efflux of Xenopus laevis oocytes expressing human P-glycoprotein
verapamil
-
inhibition of P-gp enhances the suppressive effect of kaempferol on aryl hydrocarbon receptor (AhR) transformation through an increase in the intracellular kaempferol concentration
verapamil
-
PgP inhibitors increase uptake of doxorubicin in tumor cells close to blood vessels, have little effect on drug uptake into tumor cells at intermediate distances, and might have a paradoxical effect to decrease doxorubicin uptake into distal tumor cells. This effect probably contributes to the limited success of PgP inhibitors in clinical trials
verapamil
inhibits transport of doxorubicin by a non-competitive mechanism
vinblastine
-
higher concentrations of vinblastine prevent the transport of Hoechst 33342, but low concentrations stimulate the transport of Hoechst 33342
additional information
-
the enzyme is inhibited by the transported substrates
-
additional information
not inhibited by carbonyl cyanide m-chlorophenylhydrazone and quinine
-
additional information
-
SDS, Triton X-100, urea, EGTA, EDTA, DTT and 1,10-phenanthroline have no significant effect on activity
-
additional information
-
ATPase activity associated with P-glycoprotein is characterized by three drug-dependent phases: basal without drug, drug-activated, and drug-inhibited
-
additional information
-
flavonoids inhibit the MRP1-mediated efflux of fluorescent substrate both from human erythrocytes and MDA-MB-231 resistant breast cancer cells, enzyme molecular modeling, overview
-
additional information
-
inhibitor effects on daunorubicin resistance and cell growth, overview
-
additional information
-
the main mechanisms of P-gp inhibitors involves the regulation of P-gp expression by binding to drug binding sites or modulator binding sites
-
additional information
-
CACO-2 cell monolayer experiments preincubated with the nonionic surfactant TPGS 1000 (D-alpha-tocopheryl polyethylene glycol 1000 succinate), produce stronger substrate inhibitory activity than those conducted by direct substrate and surfactant coapplication. TPGS 1000 does not function as a competitive inhibitor in P-gp substrate efflux transport
-
additional information
the enzyme is not inhibited by 4, 40, and 70 kDa dextrans, dextran sulfate Sul-D40, and the individual saccharide components of dextran (maltose, isomaltose, D-glucose)
-
additional information
the enzyme is not inhibited by 4, 40, and 70 kDa dextrans, dextran sulfate Sul-D40, and the individual saccharide components of dextran (maltose, isomaltose, D-glucose)
-
additional information
the enzyme is not inhibited by 4, 40, and 70 kDa dextrans, dextran sulfate Sul-D40, and the individual saccharide components of dextran (maltose, isomaltose, D-glucose)
-
additional information
-
acetaminophen, (acetaminophen)glucuronide, (acetaminophen)N-acetylcysteine, and (acetaminophen)sulfate do not manifest any significant inhibition
-
additional information
-
ethynylestradiol selectively diminishes the expression of Mdr2 in the intestine, no inhibition of expression of breast cancer resistance protein, of Mrp3, and expression of multidrug resistance protein 1 is only minimally impaired
-
additional information
not inhibited by rhodamine 123, rhodamine 6G, rhodamine B, quinine, and tetramethylrhodamine
-
additional information
-
not inhibited by rhodamine 123, rhodamine 6G, rhodamine B, quinine, and tetramethylrhodamine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,13-bis[4'-(4H-chromen-4-on-2-yl)phenyl]-N-(benzyl)-1,4,10,13-tetraoxa-7-azatridecane
-
stimulates ATPase activity by 2.7-fold
3,6-bis(dimethylamino)-9-(3-phenoxypropyl)-thioxanthylium hexafluorophosphate
-
-
3,6-bis(dimethylamino)-9-(N,N-diethyl-5-thiophene-2-carboxamide)selenoxanthylium hexafluorophosphate
-
-
3,6-bis(dimethylamino)-9-(N,N-diethyl-5-thiophene-2-carboxamide)thioxanthylium hexafluorophosphate
-
-
3-doxyl-17beta-hydroxy-5alpha-androstane
-
stimulation of ATPase-activity arising from co-expression of isoforms ABCG5 and ABCG8
4-androstene-3,17-dione
-
stimulation of ATPase-activity arising from co-expression of isoforms ABCG5 and ABCG8
5-androsten-3beta-ol-17-one
-
stimulation of ATPase-activity arising from co-expression of isoforms ABCG5 and ABCG8
actinomycin D
1 mM increases the ATPase activity of the enzyme more than 5times
auraptene
-
stimulates the ATPase activity of MRP1. No inhibition of MRP1-mediated efflux by auraptene, but auraptene increases the accumulation of daunorubicin in KB-C2 cells
Chlordiazepoxide
-
stimulation of ATPase activity, no effect on daunorubicin efflux
cholesterol
-
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
Diazoxide
-
about 55% increase in ATPase activity, half-activation concentration is 0.6 mM
diclofenac
-
MRP2-mediated transport of amphipathic lipophilic drugs, stimulates paclitaxel, docetaxel, and saquinavir transport
dipyridamole
1 mM increases the ATPase activity of the enzyme more than 5times
estrone glucuronide
-
the transport substrate stimulates the ATPase activity of MRP2
Estrone sulfate
-
the transport substrate stimulates the ATPase activity of MRP2
glibenclamide
-
augments the ATPase activity with a maximum attained near 100 microM
L-gamma-glutamyl-S-methyl-L-cysteinylglycine
-
supports transport of vincristine
methotrexate
-
the transport substrate stimulates the ATPase activity of MRP2
methoxypolyethylene17 glycol-beta-caprolactone5
-
amphiphilic diblock copolymer, decreases membrane fluidity and inhibits enzyme-mediated efflux while stimulating the enzyme's ATPase activity up to 3fold
MK571
-
slightly activates E217betaG activated ATPase activity of MRP3 at 0.01-0.05 mM and N-ethylmaleimide S-glutathione activated ATPase activity of MRP1 at 500-2000 nM, but inhibits MRP1 activity half-maximally at 0.01 mM, MK571 may be a potential transported substrate for MRP3, 20% stimulation of E217betaG uptake by MRP1 at 500-1000 nM, but inhibits this activity at 0.01-0.05 mM, stimulates E217betaG uptake by MRP3 at 0.002-0.005 mM, but inhibits this activity at 0.05-0.1 mM
monensin
-
protein concentration of enzyme is inversely related to the maximum activation of ATPase activity achieved
nobiletin
-
a chemopreventive citrus phytochemical from orange, stimulates the ATPase activity of MRP1. Nobiletin also increases the accumulation of calcein, a fluorescent substrate of MRP1, in KB/MRP cells
P1075
-
about 55% increase in ATPase activity, half-activation concentration is 0.036 mM
paclitaxel
1 mM increases the ATPase activity of the enzyme more than 5times
probenecid
-
the transport substrate stimulates the ATPase activity of MRP2
progesterone
1 mM increases the ATPase activity of the enzyme more than 5times
quinidine
-
protein concentration of enzyme is inversely related to the maximum activation of ATPase activity achieved
rhodamine derivatives
-
enhancement of calcein uptake into MDCK-MDR1 cells by diverse rhodamine analogues, detailed overview
-
rosamine derivatives
-
enhancement of calcein uptake into MDCK-MDR1 cells by diverse rosamine analogues, detailed overview
-
schisandrol A
-
isolated from fruit of Schisandra chinensis. Increases cellular retention of P-glycoprotein substrates such as rhodamine 123. Schisandrol A stimulates basal P-glycoprotein ATPase activity, is not competitive to verapamil or progesterone and decreases their Km value without changing Vmax values
SR47063
-
100% increase in ATPase activity, half-activation concentration is 1.5 mM
tariquidar
the substrate inhibits P-gp ATPase activity in membranes, but stimulates ATPase activity when purified P-gp is assayed in the presence of n-dodecyl-beta-D-maltoside/sheep brain lipids. Tariquidar activates the enzyme in presence of lipids, overview
tetrahydrocurcumin
-
inhibitory to P-glycoprotein as well as to mitoxantrone resistance protein and multidrug resistance protein1. Inhibition of transport function with concomitant up to 2.6fold stimulation of ATPase activity
Tolbutamide
-
increases ATPase activity, with maximum activation levels of 70%
trans,trans-4,17(20)-pregnadiene-3,16-dione
-
i.e. z-guggulsterone, stimulation of ATPase activity, inhibitory to substrate transport
valinomycin
1 mM increases the ATPase activity of the enzyme more than 5times
benzbromarone
-
slightly activates E217betaG activated ATPase activity of MRP3 at 0.01-0.03 mM, benzbromarone may be a potential transported substrate for MRP3, greatly stimulates E217betaG uptake by MRP3 at 0.001-0.02 mM, but inhibits this activity at 0.05 mM
Colchicine
-
activates the transport of tetramethylrosamine, probably by a positive allosteric effect
glutathione
-
5 mM free GSH activates the indomethacin transport by MRP1, no effect on the other substrates tested or on MRP3 activity
GSH
-
transport of unconjugated chemotherapeutic agents requires cotransport of glutathione, GSH by itself is not a substrate
methylparathion
-
0.05 mM, stimulates ATPase activity by 30% and inhibits at higher concentrations
verapamil
-
protein concentration of enzyme is inversely related to the maximum activation of ATPase activity achieved
verapamil
-
the substrate is one of the most potent activators of P-gp ATPase activity, but inhibits calcein uptake
verapamil
verapamil activates the enzyme in presence of lipids, overview. When wild-type human P-gp is expressed in Sf9 insect cells and the membranes are assayed for activity in the absence or presence of saturating concentrations of verapamil, verapamil activates ATPase activity by 4.7fold
vinblastine
-
moderate stimulation of ATPase activity, low concentrations of vinblastine stimulate the transport of Hoechst 33342, but higher concentrations prevent the transport of Hoechst 33342
vinblastine
-
the transport substrate stimulates the ATPase activity of MRP2
additional information
-
ligands of sulfonylurea receptor SUR also interact with P-plycoprotein, due to structural similarity between drug binding domains in the two proteins
-
additional information
-
elevated levels of hepatic MRP4 are found after hepatotoxicant exposure, probably mediated via transcription factor NFE2-related factor 2. Human cells upregulate MRP4 after long-term exposure to nucleoside-based drugs
-
additional information
-
praziquantel, a drug used against schistosomiasis, transiently induces expression of SMDR2 in adult worms
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00019
dimethylarsenic acid[side 1]
wild type enzyme, at 37°C, pH not specified in the publication
0.021
ethidium bromide/in
in the presence of ATP, at pH 7.5 and 37°C
0.00078
Hoechst 33342/in
in the presence of ATP, at pH 7.5 and 37°C
0.00006
N-(2'-deoxy-beta-D-ribofuranosyl)-5-cyclohexyl-1H-indole/in
-
37°C, pH not specified in the publication
0.078
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]thiochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
pH 7.4, 37°C
0.0004
nicardipine[side 1]
mutant enzyme W114Y/W161Y/W363Y/W364Y/M391W, at pH 7.5 and 37°C
0.021
tetraphenylphosphonium[side 1]
mutant enzyme W114Y/W161Y/W363Y/W364Y/M391W, at pH 7.5 and 37°C
0.075
17beta-estradiol 17-(beta-D-glucuronide)
-
pH 7.0, 37°C, recombinant MRP2
0.016
17beta-glucuronosyl [6,7-3H]oestradiol
-
vesicles from MRP3-Arg1297His transfected cells
0.0009
ATP
-
pH 7.5, 37°C, paclitaxel-stimulated ATPase activity, presence of 20% ergosterol
0.001
ATP
-
pH 7.5, 37°C, paclitaxel-stimulated ATPase activity, presence of 20% campesterol
0.0011
ATP
-
pH 7.5, 37°C, paclitaxel-stimulated ATPase activity, presence of 20% sitosterol
0.0014
ATP
-
pH 7.5, 37°C, paclitaxel-stimulated ATPase activity, presence of 20% stigmasterol
0.0016
ATP
-
pH 7.5, 37°C, paclitaxel-stimulated ATPase activity, presence of 20% cholesterol
0.004
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(N,N-diethyl-5-thiophene-2-carboxamide)thioxanthylium hexafluorophosphate
0.006
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(N,N-diethyl-5-thiophene-2-carboxamide)selenoxanthylium hexafluorophosphate
0.007
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(3-methoxyphenyl)-xanthylium hexafluorophosphate
0.009
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(3-phenoxypropyl)-thioxanthylium hexafluorophosphate
0.018
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(3-aminophenyl)-thioxanthylium hexafluorophosphate
0.07
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-phenyl-thioxanthylium bromide
0.074
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-phenyl-selenoxanthylium bromide
0.284
ATP
-
mutant enzyme Q475A, in the absence of nicardipine, at 37°C, pH not specified in the publication
0.327
ATP
-
wild type enzyme, in the absence of nicardipine, at 37°C, pH not specified in the publication
0.5
ATP
-
22°C, pH 7.4, activation by ethylparaoxon (0.03 mM) or fenvalerate (0.03 mM)
0.573
ATP
-
mutant enzyme Q1118A, in the absence of nicardipine, at 37°C, pH not specified in the publication
0.746
ATP
-
wild type enzyme, in the presence of 0.05 mM nicardipine, at 37°C, pH not specified in the publication
2.34
ATP
-
mutant enzyme Q1118A, in the presence of 0.05 mM nicardipine, at 37°C, pH not specified in the publication
2.37
ATP
-
mutant enzyme Q475A, in the presence of 0.05 mM nicardipine, at 37°C, pH not specified in the publication
0.00039
doxorubicin/in
in the presence of ATP, at pH 7.5 and 37°C
0.0011
rhodamine 6G[side 1]
mutant enzyme W114Y/W161Y/W363Y/W364Y/M391W, at pH 7.5 and 37°C
0.0031
rhodamine 6G[side 1]
mutant enzyme W114Y/W161Y/W363Y/W364Y, at pH 7.5 and 37°C
0.0038
rhodamine 6G[side 1]
wild type enzyme, at pH 7.5 and 37°C
0.1455
vinblastine/in
-
25°C, pH 7.5, vinblastine efflux by MDR1-expressing oocytes
0.0346
[1,2,6,7-3H(N)]dehydroepiandrosterone-3-sulfate/in
-
vesicles from MRP3-Arg1297His transfected cells
-
0.0463
[1,2,6,7-3H(N)]dehydroepiandrosterone-3-sulfate/in
-
vesicles from MRP3 cells
-
additional information
additional information
-
KD-values for several drugs
-
additional information
additional information
-
kinetic data, kinetic model of drug transport
-
additional information
additional information
-
kinetic data, kinetic model of drug transport
-
additional information
additional information
-
dissociation constants of transported substrates, effect of cholesterol on ATP and drug binding to reconstituted Pgp, overview
-
additional information
additional information
-
kinetics and substrate specificities, overview
-
additional information
additional information
-
Km values for stimulating rhodamine and rosamine derivatives, overview
-
additional information
additional information
-
substrate specificity, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.189
ATP
-
pH 7.4, 37°C, native enzyme, value for basal ATPase activity with no transport substrate
2.38
ATP
-
pH 7.4, 37°C, trypsin-cleaved enzyme, value for basal ATPase activity with no transport substrate
2.95
ATP
-
pH 7.4, 37°C, chymotrypsin-cleaved enzyme, value for basal ATPase activity with no transport substrate
additional information
additional information
-
MRP3 has a lower turnover rate than MRP1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
(2aR,6aR,12bS,14bS)-10,17-dimethoxy-3,3,6,6-tetramethyl-2a,3,6a,7,12b,14b-hexahydro-2H,6H-chromeno[3,4-c]chromeno[4',3':4,5]pyrano[3,2-h]chromene-13,14-dione
-
recombinant MDR1in NIH-3T3 cells
0.00042
(2aR,6aS,12bR,14bS)-10,17-dimethoxy-3,3,6,6-tetramethyl-2a,3,6a,7,12b,14b-hexahydro-2H,6H-chromeno[3,4-c]chromeno[4',3':4,5]pyrano[3,2-h]chromene-13,14-dione
-
recombinant MDR1in NIH-3T3 cells
0.00077
(2R,4aR,7bR,9R,11aR,14bR)-2,5,5,9,12,12-hexamethyl-1,3,4,4a,5,8,9,10,11,11a,12,14b-dodecahydrobenzo[c]isochromeno[3,4-g]chromene-7,14(2H,7bH)-dione
-
recombinant MDR1in NIH-3T3 cells
0.001
(6aS,9bR,15aS,18bR)-2,4,11,13-tetrabromo-7,7,16,16-tetramethyl-6a,15a,16,18b-tetrahydro-6H,15H-chromeno[3,4-c]chromeno[4',3':4,5]pyrano[2,3-g]chromene-9,18(7H,9bH)-dione
-
recombinant MDR1in NIH-3T3 cells
0.00051
(6aS,9bR,15aS,18bR)-3,12-dimethoxy-7,7,16,16-tetramethyl-6a,15a,16,18b-tetrahydro-6H,15H-chromeno[3,4-c]chromeno[4',3':4,5]pyrano[2,3-g]chromene-9,18(7H,9bH)-dione
-
recombinant MDR1in NIH-3T3 cells
0.00028 - 0.00034
1,13-bis[4'-(4H-chromen-4-on-2-yl)phenyl]-N-(benzyl)-1,4,10,13-tetraoxa-7-azatridecane
-
at 37°C, pH not specified in the publication
0.008
3,6-bis(dimethylamino)-9-(4-dimethylaminophenyl)-thioxanthylium hexafluorophosphate
-
pH 7.4, 37°C
1.6
AMP-imidodiphosphate
-
pH 7.5, 37°C, sigmoidal inhibition plot, Hill coefficient n=1.77
0.0062
clotrimazole
mutant enzyme W114Y/W161Y/W363Y/W364Y/M391W, at pH 7.5 and 37°C
0.007
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
pH 7.4, 37°C
0.002
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]thiochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
pH 7.4, 37°C
0.000004
beauvericin
-
enzyme in plasma membrane, at pH 9.5 and 30°C
additional information
additional information
-
data for drug inhibition of the basal ATPase activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00051
(1E,4E)-1,5-bis[3,4-bis(methoxymethoxy)phenyl]penta-1,4-dien-3-one
Homo sapiens
at 37°C, pH not specified in the publication
0.00031
(1E,4E)-1-(4-hydroxy-3,5-dimethoxyphenyl)-5-(3,4,5-trimethoxyphenyl)penta-1,4-dien-3-one
Homo sapiens
at 37°C, pH not specified in the publication
0.00025
(1Z,4E)-1,5-bis[3,5-bis(methoxymethoxy)phenyl]-2-chloropenta-1,4-dien-3-one
Homo sapiens
at 37°C, pH not specified in the publication
0.00037
(1Z,4E)-5-[3,5-bis(methoxymethoxy)phenyl]-2-bromo-1-[2-bromo-3,5-bis(methoxymethoxy)phenyl]penta-1,4-dien-3-one
Homo sapiens
at 37°C, pH not specified in the publication
0.0028
(2E,4E)-8-methyl-2,4-bis[(pyridin-4-yl)methylidene]-8-azabicyclo[3.2.1]octan-3-one
Homo sapiens
-
pH and temperature not specified in the publication
0.16
2-[4-(3-ethoxy-1-propenyl)phenyl]-4,5-bis-[4-(2-propylamino)phenyl]-1H-imidazole
Homo sapiens
-
pH and temperature not specified in the publication
0.0003 - 0.0016
bis[(4aS,6R,8aS)-3-methoxy-11-methyl-5,6,9,10,11,12-hexahydro-4aH-[1]benzofuro[3a,3,2-ef][2]benzazepin-6-yl] decanedioate
0.000000043
desloratadine
Homo sapiens
-
weakly inhibits daunorubicin transport, 19% of the inhibition caused by vanadate, IC50: 0.043 nM, desloratadine is no significant inhibitor of P-gp and should not cause clinical drug interactions with agents that are P-gp substrates
0.000000011
loratadine
Homo sapiens
-
inhibits daunorubicin transport, IC50: 0.011 nM, much less inhibitory than cyclosporin A or verapamil, 43% of the inhibition caused by vanadate
0.0023
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
Homo sapiens
-
pH 7.4, 37°C, recombinant enzyme
0.0053 - 0.009
N-[6-(dimethylamino)-9-[5-(piperidin-1-ylcarbonyl)thiophen-2-yl]-3H-telluroxanthen-3-ylidene]-N-methylmethanaminium hexafluorophosphate
0.0079
N-[6-(dimethylamino)-9-[5-(piperidin-1-ylcarbonyl)thiophen-2-yl]-3H-thioxanthen-3-ylidene]-N-methylmethanaminium hexafluorophosphate
Homo sapiens
-
pH 7.4, 37°C, recombinant enzyme
0.0236
N-[9-[3-(dimethylamino)phenyl]-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene]-N-methylmethanaminium bromide
Homo sapiens
-
pH 7.4, 37°C, recombinant enzyme
0.0068
N-[9-[4-(dimethylamino)phenyl]-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene]-N-methylmethanaminium bromide
Homo sapiens
-
pH 7.4, 37°C, recombinant enzyme
0.21
5'-O-[4-(fluorosulfonyl)benzoyl]adenosine
Homo sapiens
-
hydrolysis of ATP, pH 7.5, 37°C
0.68
5'-O-[4-(fluorosulfonyl)benzoyl]adenosine
Homo sapiens
-
binding of 8-azido-ATP, pH 7.5, 37°C
0.134
beta-sitosterol-O-glucoside
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in leukaemia cell line CEM/ADR5000
0.338
beta-sitosterol-O-glucoside
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in CACO-2 cells
0.0003
bis[(4aS,6R,8aS)-3-methoxy-11-methyl-5,6,9,10,11,12-hexahydro-4aH-[1]benzofuro[3a,3,2-ef][2]benzazepin-6-yl] decanedioate
Homo sapiens
-
22°C, pH 7.4, inhibition of verapamil efflux in MCF-7/DX1 (breast adenocarcinoma) cells that over-express P-gp
0.0005
bis[(4aS,6R,8aS)-3-methoxy-11-methyl-5,6,9,10,11,12-hexahydro-4aH-[1]benzofuro[3a,3,2-ef][2]benzazepin-6-yl] decanedioate
Homo sapiens
-
22°C, pH 7.4, inhibition of doxorubicin efflux in MCF-7/DX1 (breast adenocarcinoma) cells that over-express P-gp
0.0006
bis[(4aS,6R,8aS)-3-methoxy-11-methyl-5,6,9,10,11,12-hexahydro-4aH-[1]benzofuro[3a,3,2-ef][2]benzazepin-6-yl] decanedioate
Homo sapiens
-
22°C, pH 7.4, inhibition of rhodamine 123 efflux in MCF-7/DX1 (breast adenocarcinoma) cells that over-express P-gp
0.0016
bis[(4aS,6R,8aS)-3-methoxy-11-methyl-5,6,9,10,11,12-hexahydro-4aH-[1]benzofuro[3a,3,2-ef][2]benzazepin-6-yl] decanedioate
Homo sapiens
-
22°C, pH 7.4, inhibition of daunomycin efflux in MCF-7/DX1 (breast adenocarcinoma) cells that over-express P-gp
0.003
coumermycin A1
Streptococcus pneumoniae
-
mutant enzyme Q521A, with ATP as cosubstrate, at pH 7.0 and 30°C
0.0031
coumermycin A1
Streptococcus pneumoniae
-
wild type enzyme, with GTP as cosubstrate, at pH 7.0 and 30°C
0.0034
coumermycin A1
Streptococcus pneumoniae
-
mutant enzyme Q521A, with ATP as cosubstrate, at pH 7.0 and 30°C
0.0037
coumermycin A1
Streptococcus pneumoniae
-
wild type enzyme, with ATP as cosubstrate, at pH 7.0 and 30°C
0.0161
curcumin
Homo sapiens
-
with calcein as substrate, pH and temperature not specified in the publication
0.0169
curcumin
Homo sapiens
-
with 2,7-bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein as substrate, pH and temperature not specified in the publication
0.0004
D-alpha-tocopheryl polyethylene glycol 1000 succinate
Homo sapiens
-
37°C, presence of nicardipine
-
0.00082
D-alpha-tocopheryl polyethylene glycol 1000 succinate
Homo sapiens
-
37°C, presence of quinidine
-
0.00318
D-alpha-tocopheryl polyethylene glycol 1000 succinate
Homo sapiens
-
37°C, presence of verapamil
-
0.00325
D-alpha-tocopheryl polyethylene glycol 1000 succinate
Homo sapiens
-
37°C, presence of progesterone
-
0.22
deacetylnomilin
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in leukaemia cell line CEM/ADR5000
0.478
deacetylnomilin
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in CACO-2 cells
0.0065
ethidium
Streptococcus pneumoniae
-
mutant enzyme Q521A, with ATP as cosubstrate, at pH 7.0 and 30°C
0.0071
ethidium
Streptococcus pneumoniae
-
wild type enzyme, with ATP as cosubstrate, at pH 7.0 and 30°C
0.0227
ethidium
Streptococcus pneumoniae
-
wild type enzyme, with GTP as cosubstrate, at pH 7.0 and 30°C
0.0303
ethidium
Streptococcus pneumoniae
-
mutant enzyme Q521A, with ATP as cosubstrate, at pH 7.0 and 30°C
0.195
hesperidin
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in CACO-2 cells
0.23
hesperidin
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in leukaemia cell line CEM/ADR5000
0.285
limonin
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in leukaemia cell line CEM/ADR5000
0.52
limonin
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in CACO-2 cells
0.0053
N-[6-(dimethylamino)-9-[5-(piperidin-1-ylcarbonyl)thiophen-2-yl]-3H-telluroxanthen-3-ylidene]-N-methylmethanaminium hexafluorophosphate
Homo sapiens
-
pH 7.4, 37°C, recombinant enzyme
0.009
N-[6-(dimethylamino)-9-[5-(piperidin-1-ylcarbonyl)thiophen-2-yl]-3H-telluroxanthen-3-ylidene]-N-methylmethanaminium hexafluorophosphate
Homo sapiens
-
pH 7.4, 37°C, recombinant enzyme
0.169
neohesperidin
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in leukaemia cell line CEM/ADR5000
0.174
neohesperidin
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in CACO-2 cells
0.0046
novobiocin
Streptococcus pneumoniae
-
wild type enzyme, with ATP as cosubstrate, at pH 7.0 and 30°C
0.0065
novobiocin
Streptococcus pneumoniae
-
mutant enzyme Q521A, with ATP as cosubstrate, at pH 7.0 and 30°C
0.0066
novobiocin
Streptococcus pneumoniae
-
wild type enzyme, with GTP as cosubstrate, at pH 7.0 and 30°C
0.0097
novobiocin
Streptococcus pneumoniae
-
mutant enzyme Q521A, with ATP as cosubstrate, at pH 7.0 and 30°C
0.0009
propidium
Streptococcus pneumoniae
-
wild type enzyme, with ATP as cosubstrate, at pH 7.0 and 30°C
0.0009
propidium
Streptococcus pneumoniae
-
mutant enzyme Q521A, with ATP as cosubstrate, at pH 7.0 and 30°C
0.001
propidium
Streptococcus pneumoniae
-
wild type enzyme, with GTP as cosubstrate, at pH 7.0 and 30°C
0.0023
propidium
Streptococcus pneumoniae
-
mutant enzyme Q521A, with ATP as cosubstrate, at pH 7.0 and 30°C
0.21
stigmasterol
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in leukaemia cell line CEM/ADR5000
0.387
stigmasterol
Homo sapiens
-
37°C, pH is not specified in the publication. Rhodamine 123 efflux assay, in CACO-2 cells
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0265
-
recombinant enzyme in presence of verapamil and doxorubicin, ATPase activity
0.0289
-
recombinant enzyme in presence of naringin and doxorubicin, ATPase activity
1.7
-
purified recombinant wild-type MDR1, ATPase activity with substrate verapamil
additional information
additional information
-
substrate specificities of transmembrane segment mutants, overview
additional information
-
relative drug resistance factor of wild-type MRP1and MRP3, and mutants, overview. Transport activities of wild-type MRP1 and of the mutant hybride MRP1/MRP3 prepared from Sf21 cells, overview
additional information
-
relative activities and substrate specificity of wild-type an dmutant enzymes
additional information
-
activities of purified wild-type and mutant enzymes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.4 - 7.5
7.4 - 8.1
-
assay at, dependent on the solubility of participating components of the reconstituting proteoliposomes
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35 - 37
37
37
-
assay at
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
pattern of temperature dependence of the rate of tetramethylrosamine transport by Pgp, the transport rate is relatively high in the rigid gel phase, reaches a maximum at the melting temperature of the bilayer, and then decreases in the fluid liquid crystalline phase
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SMDR2, Egyptian isolate propagated in female Swiss Webster mice
-
-
brenda
-
210381, 210382, 210383, 210385, 210386, 210387, 210388, 210394, 210399, 210400, 210401, 210402, 657552, 657840, 658514, 659188, 659295, 660405, 660546, 667719, 667817, 668705, 669989, 670491, 685022, 685450, 686564, 688594, 689065, 689695, 689698, 696129, 696343, 697106, 697110, 697202, 697583, 697586, 697712, 697760, 697766, 698233, 699450, 699712, 700297, 701069, 701356, 701435, 710872, 711073, 711157, 711411, 711558, 711656, 711753, 711833, 711893, 711926, 711931, 711932, 711970, 712696, 712710, 713065, 713066, 713201, 713202, 713592, 718735, 718802, 718806, 718864, 718899, 718964
-
-
brenda
-
720035, 720192, 720505, 733255, 733332, 733539, 733820, 734280, 734441, 734442, 735307, 746663, 747041
-
-
brenda
human multidrug resistance gene MDR1 encoding a membrane-bound transporter P-glycoprotein
Uniprot
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
plasma membrane vesicles from brain microvessel endothelial cells
brenda
-
MRP3 is the predominant MRP isoform in cholangiocellular carcinomas (57%), whereas MRP2 is undetectable in cholangiocellular carcinomas
brenda
-
inside-out plasma membrane vesicles of MDR1-transfected mouse embryo fibroblasts (NIH-MDR1-G185)
brenda
-
MRP3 is the predominant MRP isoform in gallbladder carcinomas (93%), whereas MRP2 expression is detected in only 29% of gallbladder carcinomas
brenda
apical side of the intestinal epithelium
brenda
-
constitutive expression of MDR P-glycoproteins, MRP1, MRP2 and MRP3 in Mz-ChA-1 cells. MRP2 and MRP3 are expressed in the respective apical and basolateral membrane domains, isozyme expression analysis amd immunohistochemic localization analysis, overview
brenda
-
cell line overexpressing the cloned human MDR1 gene product
brenda
-
fish hepatoma cells characterized by high overexpression of P-glycoprotein
brenda
additional information
-
MRP4 is mainly expressed in the luminal membrane of capillary endothelium, but also in the basolateral membrane of choroid plexus and in astrocytes
brenda
-
endothelium and epithelium, immunohistochemic localization
brenda
-
selected from spontaneously transformed Chinese hamster lung fibroblast DC-3F on the basis of resistance to actinomycin D
brenda
-
Mrp3 is located in the basolateral, Bcrp1 in the apical membranes of enterocytes
brenda
-
293 human embryonic kidney cells and Madin-darby canine kidney II cells transfected with a MRP5 cDNA construct
brenda
-
localisation of MRP4 to the apical membrane of kidney proximal tubules
brenda
-
MRP4 expression is highly variable and is transcriptionally regulated through the constitutive androstane receptor
brenda
-
isoform Abcb5 is detected in earlier follicular stages of the ovary
brenda
-
placental apical membrane, preparation of brush border membrane inside-out vesicles
brenda
additional information
-
tissue-specific expression of monkey MRP2, no expression in cerebrum and colon
brenda
additional information
-
isozymes Mdr1a and Mdr1b show a developmental pattern of low expression at birth, followed by a gradual increase to mature levels at approximately 30 days of age in all tissues. In contrast, Mdr2 mRNA in liver is markedly up-regulated at birth, which returns to low levels by 5 days of age and then gradually increases to mature levels. The three Mdr transporters in mice are expressed in a tissue-specific and age-dependent pattern, there are gender differences in expression, and Mdr transporters are inducible by only a few microsomal enzyme inducers
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
recombinant P-glycoprotein, expressed in Saccharomyces cerevisiae proteoliposome
-
brenda
-
recombinant YvcC is highly enriched in membrane vesicles and embedded in the membrane in a fully functional conformation
brenda
-
contains an additional third NH2-proximal membrane-spanning domain, not found in previously characterized ABC transporters. This domain, whose NH2-terminus is extracytolsolic, is essential for MRP-mediated transport activity
brenda
-
MRP1 possesses three transmembrane domains, TMD0, TMD1, and TMD2
brenda
-
MRP4 shows a dual membrane localisation in polarised cell types
brenda
-
P-gp possesses a linker region of about 75 amino acids that connects two homologous halves, each of which contain a transmembrane domain followed by a nucleotide-binding domain
brenda
a transmembrane enzyme with 12 transmembrane segments
brenda
the homodimeric protein consists of 12 transmembrane helices, and integral membrane protein
brenda
-
the homodimeric protein consists of 12 transmembrane helices, and integral membrane protein
-
brenda
-
the homodimeric protein consists of 12 transmembrane helices, and integral membrane protein
-
brenda
-
transmembrane protein, location in the membrane
brenda
-
intimate association of both Pgp and its substrates with the membrane, dependence of the rate of tetramethylrosamine transport by Pgp on the bilayer phase state, the transport rate is relatively high in the rigid gel phase, reaches a maximum at the melting temperature of the bilayer, and then decreases in the fluid liquid crystalline phase
brenda
-
MDR1 encodes a 170 kDa integral plasma membrane protein
brenda
-
recombinant Pgp, expressed in Saccharomyces cerevisiae
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
the enzyme is a lipophilic anion transporter that pumps endogenous and xenobiotic substrates from the cytoplasm to the extracellular milieu
physiological function
additional information
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
malfunction
-
knockdown of enzyme expression reverses progesterone- and deoxycorticosterone-induced collateral sensitivity of CHO cells
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
malfunction
-
enzyme deletion results in increased susceptibility to daunorubicin, doxorubicin, ethidium, and Hoechst 33342
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
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
-
malfunction
-
enzyme deletion results in increased susceptibility to daunorubicin, doxorubicin, ethidium, and Hoechst 33342
-
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
physiological function
-
overexpression of P-gp is often associated with multidrug resistance, as it can efflux a wide range of large hydrophobic and amphiprotic substrates
physiological function
-
mediates drug efflux from cells and plays a major role in causing multidrug resistance
physiological function
-
the enzyme can actively pump drugs out of cells conferring the phenotype of multidrug resistance
physiological function
-
P-glycoprotein conveys multidrug resistance. It is an ATP-dependent drug efflux pump that transports a wide variety of structurally unrelated compounds out of cells
physiological function
-
the human multidrug resistance transporter P-glycoprotein prevents the entry of compounds into the brain by an active efflux mechanism at the blood-brain barrier
physiological function
-
the presence of Pgp could be one of the reasons for insecticide resistance in this pest
physiological function
-
P-gp in the membrane is in the closed conformation that has a high affinity for drug substrates
physiological function
-
the enzyme is a major player in multidrug resistance
physiological function
-
the enzyme confers resistance to growth inhibitory concentrations of ethanol. Enzyme expression decreases intracellular ethanol accumulation and ethanol-induced plasma membrane permeabilization
physiological function
-
the enzyme mediates collateral sensitivity of multidrug resistance cells in the presence of physiologically achievable concentrations of progesterone and deoxycorticosterone
physiological function
the enzyme plays a vital and dispensable role during blood stages. Isoforms MDR2 and MDR5 have important functions in sporogony as well as sporozoite development
physiological function
-
the enzyme plays a vital and dispensable role during blood stages. Isoforms MDR2 and MDR5 have important functions in sporogony as well as sporozoite development
physiological function
the enzyme ABCG2 protects tissues against xenobiotics, affects the pharmacokinetics of drugs and contributes to multidrug resistance
physiological function
the enzyme may be responsible for chemotherapy failure and tumor relapse in patients with head and neck squamous cell carcinoma
physiological function
the enzyme plays a vital and dispensable role during blood stages
physiological function
the localization of enzyme ABCG2 can play a vital role in limiting absorption (in the small intestine), mediating distribution (e.g. in the blood-brain and blood-placental barriers) and facilitating elimination and excretion (in the liver and kidney) of drugs or xenobiotics
physiological function
multidrug transporters of the ABC family facilitate the export of diverse cytotoxic drugs across cell membranes
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
physiological function
-
the enzyme has a critical role in conferring antibiotic resistance in multidrug-resistant infections by Streptococcus pneumoniae
physiological function
the enzyme is a major key player in cancer-related multidrug resistance. The enzyme is related to the glutathione content of cells and contributes to the beta-amyloid protein clearance in Alzheimer's disease
physiological function
-
the increase of the enzyme positively modulates the cell chemoresistance, but decreases cell migration and proliferation
physiological function
the enzyme is a general protection mechanism to keep toxic xenobiotics from entering the body through the intestines, to excrete such xenobiotics via the kidney and liver if they are absorbed, and to protect vulnerable tissues from circulating toxins by the blood-brain, blood-testis/ovary, and placental barriers
physiological function
the enzyme actively extrudes certain xenobiotics and other amphiphiles across the plasma membrane
physiological function
the enzyme plays a major role in drug resistance by extruding out drugs and antibiotic molecules from cells
physiological function
-
the enzyme confers resistance to growth inhibitory concentrations of ethanol. Enzyme expression decreases intracellular ethanol accumulation and ethanol-induced plasma membrane permeabilization
-
physiological function
-
multidrug transporters of the ABC family facilitate the export of diverse cytotoxic drugs across cell membranes
-
physiological function
-
multidrug transporters of the ABC family facilitate the export of diverse cytotoxic drugs across cell membranes
-
additional information
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
additional information
-
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
additional information
-
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
-
additional information
-
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
-
Show AA Sequence and Transmembrane Helices (25831 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
190000
63000
1 * 63000 + 1 * 74000, YdaG +YdbA, a stable heterodimer, SDS-PAGE
74000
1 * 63000 + 1 * 74000, YdaG +YdbA, a stable heterodimer, SDS-PAGE
190000
-
1 * 190000, MRP from lung cancer cell line, calculation from nucleotide sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
homodimer
monomer
additional information
?
x * 29400, multidrug resistance-associated protein 4-nucleotide-binding domain 1, SDS-PAGE
?
-
1 * 190000, MRP from lung cancer cell line, calculation from nucleotide sequence
?
x * 46600, calculated from amino acid sequence
heterodimer
1 * 63000 + 1 * 74000, YdaG +YdbA, a stable heterodimer, SDS-PAGE
heterodimer
-
1 * 63000 + 1 * 74000, YdaG +YdbA, a stable heterodimer, SDS-PAGE
-
heterodimer
-
subunits PatA and PatB need to interact together to make a functional drug efflux transporter and work only as heterodimers
heterodimer
-
1 * 67000 + 1 * 63000, calculated from amino acid sequence
additional information
-
enzyme contains a membrane-associated domain made up of 12 alpha-helical membrane-spanning segments and two highly conserved cytosolic nucleotide-binding domains which couple ATP hydrolysis to substrate import or export
additional information
-
the P-glycoprotein contains 12 transmembrane domains with 6 extracellular loops and 2 cytoplasmic ATP-binding domains
additional information
-
MRP1 is a 190-kDa protein composed of two hydrophobic transmembrane domains, each followed by a cytoplasmic nucleotide-binding domain
additional information
-
membrane topology, MRP1 domain arrangement, structure analysis and comparison, overview
additional information
-
the enzyme structure shows multiple allosteric binding sites of MRP4, homology model of human MRP4: MRP4 has a typical ABC transporter core structure comprising two membrane-spanning domains, each consisting of six transmembrane helices with two cytosolic ATP-binding domains, which bind and hydrolyse ATP to power substrate transport
additional information
-
three-dimensional models of two different catalytic states of Pglycoprotein are developed based on the crystal structures of two bacterial multidrug transporters, molecular docking, overview
additional information
-
expression of His6-ABCG2 in Sf9 insect cells and in human Flp-In-293/ABCG2 cells both results in tetrameric organization of ABCG2
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
phosphoprotein
side-chain modification
-
contains putative phosphorylation and myristylation sites
ubiquitination
-
H1 prompts the degradation of Pgp and decreases Pgp protein half-life by enhancing the ubiquitination of Pgp
glycoprotein
-
glycosylation is not essential for ATPase or transport function, the N-linked oligosaccharides appear to influence the conformation of the protein in a subtle way
glycoprotein
-
one glycosylation site is in the second half of the P-glycoprotein, the second glycosylation site links transmembrane domains 8 and 9 in the traditional model of the P-glycoprotein topology
glycoprotein
-
P-gp is a highly glycosylated plasma membrane protein that exists in several glycoforms, with different degrees of glycosylation
glycoprotein
-
glycosylation is not essential for ATPase or transport function, the N-linked oligosaccharides appear to influence the conformation of the protein in a subtle way
glycoprotein
-
one glycosylation site is in the second half of the P-glycoprotein, the second glycosylation site links transmembrane domains 8 and 9 in the traditional model of the P-glycoprotein topology
glycoprotein
-
glycosylation is not essential for ATPase or transport function, the N-linked oligosaccharides appear to influence the conformation of the protein in a subtle way
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, native protein is crystallized by using 100 mM HEPES pH 6.6-7.2, 200 mM sodium malonate and 19-22% (w/v) PEG 2000-MME, at 4°C. Crystals of selenomethionine-substituted protein are obtained with 100 mM HEPES pH 6.6-7.2, 200 mM ammonium phosphate monobasic and 19-22% PEG 1500 at 4°C
mutant enzyme W114Y/W161Y/W363Y/W364Y/M391W , sitting drop vapor diffusion method, using 15.2% (w/v) PEG 2000 MME, 100 mM potassium nitrate, and 100 mM magnesium nitrate
mutant enzyme E25N/W31I/V34M which binds L10 monobody to facilitate crystallization, a low-pH (proton-bound) structure and five structures in complex with structurally diverse quaternary phosphonium, quaternary ammonium, and planar aromatic substrates, using 100 mM LiNO3 or 100 mM NH4SO4, 100 mM ADA, pH 6.5 or 100 mM HEPES, pH 7.1-7.3, and 30-35% PEG (w/v) 600
variant I239T/G354E in complexes with n-dodecyl-N,N-dimethylamine N-oxide, methyl viologen and deoxycholate, hanging drop vapor diffusion method, using 10 0mM MES-NaOH, pH 6.0, 200mM NaCl, 100 mM MgCl2, 40 mM praseodymium acetate, 30-40% (w/v) PEG400
homology modeling with estradiol 17-beta-D-glucuronide, cyclic guanosine monophosphate, methotrextae and folic acid as substrates
-
vapor diffusion method, using 25% (w/v) PEG 2000 MME buffered with 0.1 M Tris-HCl pH 7.0
-
in complex with Hoechst 33342, sitting drop vapor diffusion method, using 80 mM SPG pH 7.0, 20% (w/v) PEG 1500
hanging drop vapor diffusion method, using 100 mM HEPES, pH 7.5, 200 mM NaCl, 25% (w/v) PEG400
purified bacterial multidrug ABC transporter, X-ray diffraction structure determination and analysis at 3.0 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E504A
E504Q
K380A
K380R
A1208V/G521S
-
the mutant exhibits a strong synergistic decrease of resistance to fenbuconazole
A666G
-
the mutant shows an uncoupling of ATPase and drug transport and displays a selective loss of resistance to one or more of the tested drugs, the mutant displays a hyperresistant phenotype towards fluconazole comparable to wild type
C1056A
-
the mutation leads to increased drug susceptibility while the ATPase activity of the mutant remains unaltered
C1091A
-
the mutation leads to increased drug susceptibility while the ATPase activity of the mutant remains unaltered
C1106A
-
the mutation leads to increased drug susceptibility while the ATPase activity of the mutant remains unaltered
C1294A
-
the mutation leads to increased drug susceptibility while the ATPase activity of the mutant remains unaltered
C1336A
-
the mutation leads to increased drug susceptibility while the ATPase activity of the mutant remains unaltered
C193K
-
residue of the Walker A motif of the N-terminal nucleotide binding domain, mutant with 22% ATPase activity compared with native Cdr1p, mutant cells are not hypersensitive to drugs such as fluconazole, ansiomycin, miconazole or cycloheximide
C193K/K901
-
double mutant has an ATPase activity below 10% compared with native Cdr1p
C363R/G521S
-
the mutant shows an intermediate increase in resistance to resazurine and no decrease of resistance to ketoconazole
C363R/G521S/V885G/A1208V
-
the quadruple mutant almost completely loses the ability to confer cycloheximide tolerance
C363R/V885G
-
the mutant exhibits a strong synergistic decrease of resistance to fenbuconazole
D1026A
-
similar to wild-type in cell surface expression and labeling by iodoarylazidoprazosin, but severeyl impaired in ATPase activity and drug efflux
D1026N
-
similar to wild-type in cell surface expression and labeling by iodoarylazidoprazosin, but severeyl impaired in ATPase activity and drug efflux. Deficiency in nucleotide binding
D327A
-
similar to wild-type in cell surface expression and labeling by iodoarylazidoprazosin, but severeyl impaired in ATPase activity and drug efflux
D327N
-
similar to wild-type in cell surface expression and labeling by iodoarylazidoprazosin, but severeyl impaired in ATPase activity and drug efflux. At acidic pH value, 40% enhancement of residual ATPase activity
D327N/D1026N
-
similar to wild-type in cell surface expression and labeling by iodoarylazidoprazosin, but severeyl impaired in ATPase activity and drug efflux. Deficiency in nucleotide binding
F673A
-
the mutant shows a reduction in both Km and Vmax values of ATPase activity when compared to wild-type Cdr1p-GFP, and displays a selective loss of resistance to one or more of the tested drugs
G672A
-
the mutant shows an uncoupling of ATPase and drug transport and displays a selective loss of resistance to one or more of the tested drugs
I675A
-
the mutant shows a reduction in both Km and Vmax values of ATPase activity when compared to wild-type Cdr1p-GFP, and displays a selective loss of resistance to one or more of the tested drugs
K901C
-
residue of the Walker A motif of the C-terminal nucleotide binding domain, mutant with 12% ATPase activity compared with native Cdr1p, mutant cells are hypersensitive to drugs such as fluconazole, ansiomycin, miconazole or cycloheximide and are unable to expel rhodamine 6G
L663A
-
the mutant shows an uncoupling of ATPase and drug transport and displays a selective loss of resistance to one or more of the tested drugs
L664A
-
the mutant shows an uncoupling of ATPase and drug transport and displays a selective loss of resistance to one or more of the tested drugs
M667A
-
the mutant shows a reduction in both Km and Vmax values of ATPase activity when compared to wild-type Cdr1p-GFP, and displays a selective loss of resistance to one or more of the tested drugs
P659A
-
the mutant shows an uncoupling of ATPase and drug transport and displays a selective loss of resistance to one or more of the tested drugs
P676A
-
the mutant shows an uncoupling of ATPase and drug transport and displays a selective loss of resistance to one or more of the tested drugs
P678A
-
the mutant shows a reduction in both Km and Vmax values of ATPase activity when compared to wild-type Cdr1p-GFP, and displays a selective loss of resistance to one or more of the tested drugs
T671A
-
the mutant shows an uncoupling of ATPase and drug transport and displays a selective loss of resistance to one or more of the tested drugs
T677A
-
the mutant shows an uncoupling of ATPase and drug transport and displays a selective loss of resistance to one or more of the tested drugs
V668A
-
the mutant shows an uncoupling of ATPase and drug transport and displays a selective loss of resistance to one or more of the tested drugs
V674A
-
the mutant shows an uncoupling of ATPase and drug transport and displays a selective loss of resistance to one or more of the tested drugs
V885G/A1208V
-
the mutant shows an intermediate increase in resistance to resazurine and a strong synergistic decrease of resistance to fenbuconazole
C363R/G521S
-
the mutant shows an intermediate increase in resistance to resazurine and no decrease of resistance to ketoconazole
-
C363R/G521S/V885G/A1208V
-
the quadruple mutant almost completely loses the ability to confer cycloheximide tolerance
-
C363R/V885G
-
the mutant exhibits a strong synergistic decrease of resistance to fenbuconazole
-
V885G/A1208V
-
the mutant shows an intermediate increase in resistance to resazurine and a strong synergistic decrease of resistance to fenbuconazole
-
W114Y/W161Y/W363Y/W364Y
the mutant exhibits dramatically reduced background fluorescence and high sensitivity to the addition of substrates, allowing for accurate measurement of Trp fluorescence quenching upon substrate binding. Its rhodamine 6G resistance is essentially the same as the yeast strains expressing the wild type protein. The initial rate of ATPase activity of the mutant is 1.3fold higher than that of the wild type in the presence of 0.02 mM rhodamine 6G
W114Y/W161Y/W363Y/W364Y/M391W
the mutant is essentially the same as wild type and the mutant also retains its activity
W114Y/W161Y/W363Y/W364Y
-
the mutant exhibits dramatically reduced background fluorescence and high sensitivity to the addition of substrates, allowing for accurate measurement of Trp fluorescence quenching upon substrate binding. Its rhodamine 6G resistance is essentially the same as the yeast strains expressing the wild type protein. The initial rate of ATPase activity of the mutant is 1.3fold higher than that of the wild type in the presence of 0.02 mM rhodamine 6G
-
W114Y/W161Y/W363Y/W364Y/M391W
-
the mutant is essentially the same as wild type and the mutant also retains its activity
-
E512Q
A150A/I239T/G354E
the mutations exert little deleterious effect on the transport function of the enzyme
D34A/I239T/G354E
G354E
the mutation abolishes the ability of the enzyme to extrude deoxycholate
I239T/F361A/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
I239T/G354E
the mutation both broadenes (for methyl viologen) and narrows (for deoxycholate) the drug recognition spectrum of the enzyme, largely by altering the transporter-drug interactions
I239T/L339A/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
I239T/M353A/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
I239T/S350A/G354E
the mutations exert little deleterious effect on the transport function of the enzyme
I239T/V335A/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
L236A/I239T/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
L62A/I239T/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
M146A/I239T/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
M58A/I239T/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
N33A/I239T/G354E
the mutations reduce the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
S232A/I239T/G354E
the mutations exert little deleterious effect on the transport function of the enzyme
Y127A/I239T/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
Y30A/I239T/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
A481G/V482A/M483V/M485V
-
the MRP1 mutant shows altered transport activities compared to the wild-type MRP1
A493K/H494Q/S497L/N500S
-
the MRP1 mutant shows altered transport activities compared to the wild-type MRP1
A493K/H494Q/S497L/N500S/N506S
-
the MRP1 mutant shows altered transport activities compared to the wild-type MRP1
A493K/H494Q/S497L/N506S/T487M/K488R/T489A/Y490F
-
the MRP1 mutant shows altered transport activities compared to the wild-type MRP1
A80C/R741C
site-directed mutagenesis, cysteines A80C/R741C are close enough to spontaneously form a disulfide bond in the mature protein at the cell surface and trap Pgp in an inactive conformation. Tariquidar is the only P-gp drug substrate or modulator that blocks A80C/R741C crosslinking
A980C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
C137A/C431A/C717A/C956A/C1074A/C1125A/C1227A
-
replacement of the seven endogenous cysteines to create a Cys-less P-gp. Intoduction of new cysteine residues in different domains and disulfide cross-linking with short or long cross-linkers shows that cross-linking of cysteines that lie close to the LSGGQ signature sequne, such as P517C, and Walker A, such as I1050C, sites of NBD1 and NBD2 respectively, as well as thecytoplasmic extensions of TM segments 3, D177C or L175C, and 9, N820C, with a shortcross-linker activat ATPase activity over 10fold. Cross-linking between the NBDs is not inhibited by tariquidar. Cross-linking between extracellular cysteines, mutant T333C/L975C, predicted to lock P-gp into a conformation that prevents close NBD association inhibit ATPase activity
C956S
-
the mutation leads to reduced cell surface expression with unaltered total protein but does not affect the enzyme activity
D1179A
-
site-directed mutagenesis, the mutant shows similar or higher expression level, but about 35% reduced drug transport activity and altered substrate specificity compared to the wild-type enzyme
D1183E
-
site-directed mutagenesis, the mutant shows transport activities similar to the wild-type enzyme, but reduced expression level
E1144A
-
site-directed mutagenesis, the mutant shows similar or higher expression level, but about 50% reduced drug transport activity compared to the wild-type enzyme
E1184A
-
site-directed mutagenesis, the mutant shows similar or higher expression level, but reduced activity and altered substrate specificity compared to the wild-type enzyme
E556Q/E1201Q
-
Walker B mutant, traps nucleotide in the absence of vandate or beryllium fluoride. Use for identification of reaction intermediates
E936Q
-
the mutant shows slightly increases activity with taurocholic acid and estradiol 17-beta-glucuronide compared to the wild type enzyme
F343C
site-directed mutagenesis, 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
F368A
-
almost complete disruption of transport activity for all substrates tested
F368W
-
F368W-mediated estradiol 17-beta-D-glucuronide transport is increased to 250% of wild type MRP4, whereas cyclic guanosine monophosphate transport is decreased to 24% , and methotrextae and folic acid transport is reduced to 5580% of wild type transport activity
F368Y
-
F368Y-mediated cyclic guanosine monophosphate transport is increased to 160%, while transport of the other substrates is decreased by 2050% compared to wild type
F978C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
F994C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
G1433D
-
mutation in the ABC-signature region of MRP1, mutant has negligible ATPase and vesicular transport activity, but shows normal ATP-binding, no transition state formation in the ATPase catalytic cycle
G187W
-
the mutation moderately increases the enzyme activity in a substrate-dependent manner
G571A/G191R
a naturally occuring mutant, the genetic variation modulates cancer drug resistance and efflux transport, minimal effect on doxorubicin and daunorubicin, the MDR1-dependent resistance on vinblastine, vincristine, paclitaxel, and etoposide is reduced by approximately 5fold, overview
G771D
-
mutation in the ABC-signature region of MRP1, mutant has negligible ATPase and vesicular transport activity, but shows normal ATP-binding, no transition state formation in the ATPase catalytic cycle
G984C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
G989C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
I306C
site-directed mutagenesis, mutant I306C (TM5) shows highly activated ATPase activity, about 10fold greater than the untreated mutant after treatment with MTS-verapamil when labeling is performed in the presence or absence of n-dodecyl-beta-D-maltoside
I441L
-
the mutant shows reduced activity with vincristine, VP-16, and doxorubicin compared to the wild-type enzyme
K1181A
-
site-directed mutagenesis, the mutant shows similar or higher expression level compared to the wild-type enzyme
K293E
-
the mutation moderately increases the enzyme activity in a substrate-dependent manner
K304N
-
the mutant shows slightly reduced activity with taurocholic acid and estradiol 17-beta-glucuronide compared to the wild type enzyme
L1260A
site-directed mutagenesis, rescue of the L1260A processing mutant by detergents
L1430R
-
mutation in the ABC-signature region of MRP1, mutant has both ATPase and vesicular transport activity
L175C/N820C
-
introduction of cysteine residues into regions of TM3, residues 175-178, and TM9, residues 820822. Treatment with 1,1-methanediyl bismethanethiosulfonate results in cross-linking of the majority of protein. Cross-linking is not increased in the presence of ATP or drug substrates. Cross-linking increases the mutant's basal ATPase activity about 3fold. Activity can be increased further by drug substrates such as verapamil and rhodamine B
L18I
-
the mutation moderately increases the enzyme activity in a substrate-dependent manner
L768R
-
mutation in the ABC-signature region of MRP1, mutant has both ATPase and vesicular transport activity
L976C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
M443L
-
the mutant shows reduced activity with vincristine, VP-16, and doxorubicin compared to the wild-type enzyme
M443L/Y440F/1441L
-
the MRP1 mutant shows altered transport activities compared to the wild-type MRP1
M986C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
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
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
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
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
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
Q1118A
-
the mutant with 8.1% of wild type activity accumulates low levels of Bodipy-verapamil
Q141K
the mutation is associated with hyperuricemia and gout. It results in decreased expression or degradation of the protein
Q475A
-
the mutant with 9.5% of wild type activity accumulates low levels of Bodipy-verapamil
Q475A/Q1118A
-
the mutant accumulates more levels of Bodipy-verapamil compared to the wild type enzyme
Q990C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
R1166K
-
site-directed mutagenesis, the mutant shows transport activities similar to the wild-type enzyme, but reduced expression level
R1173A
-
site-directed mutagenesis, the mutant shows similar or higher expression level, but increased activity and altered substrate specificity compared to the wild-type enzyme
R1297H
-
the naturally occuring mutant protein MRP3-Arg1297His is correctly localized to the basolateral membrane and shows no significant differences in the transport of several organic anions compared to MRP3. Based on the membrane vesicle transport assays, individuals with the MRP3-Arg 1297 His variant are not expected to be affected in their ability to export MRP3 substrates into blood
R531Q
-
the mutation moderately increases the enzyme activity in a substrate-dependent manner
R998K
-
almost complete disruption of transport activity for all substrates tested
R998L
-
almost complete disruption of transport activity for all substrates tested
R998S
-
almost complete disruption of transport activity for all substrates tested
R998Y
-
almost complete disruption of transport activity for all substrates tested
S992C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
T1142M
-
the mutant shows reduced activity with taurocholic acid and estradiol 17-beta-glucuronide compared to the wild type enzyme
T2D
-
mutation of two tyrosine residues in MRP1 cannot alter the sensitivity to glibenclamide
V458M
-
the mutant with reduced cell surface expression with unaltered total protein shows reduced activity with taurocholic acid and estradiol 17-beta-glucuronide compared to the wild type enzyme
V479L/A481G/V482A/M483V/M485V
-
the MRP1 mutant shows altered transport activities compared to the wild-type MRP1
V479L/A481G/V482A/M483V/N500S
-
the MRP1 mutant shows altered transport activities compared to the wild-type MRP1
V982C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
V988C
-
site-directed mutagenesis, the mutant shows altered substrate transport activity and activation by the substrates, e.g. vinblastine and nicardipine, compared to the wild-type enzyme
W995A
-
almost complete disruption of transport activity for all substrates tested
Y440F
Y440F/1441L
-
the mutant shows reduced activity with vincristine, VP-16, and doxorubicin compared to the wild-type enzyme
N116Y
the mutant shows a greater than 5fold decrease in IC50 for tetracycline and a more than 2fold decrease in IC50 for erythromycin as compared to the wild type enzyme
S52Y
the mutant shows a greater than 4fold decrease in IC50 for tetracycline as compared to the wild type enzyme
T56Y
the mutant shows a greater than 5fold decrease in IC50 for tetracycline and a more than 2fold decrease in IC50 for erythromycin as compared to the wild type enzyme
S1034C/D1246Y
-
decrease in Km value for ATP, slightly less sensitive to vanadate than wild-type
S1034C/N1042D
-
kinetics similar to wild-type, less sensitive to vanadate
F178A
the mutation reduces antimicrobial activity in the enzyme
D1042N
-
the mutant exhibits an rhodamine 6G efflux rate that is 10% as high as that of the wild type
E574K
-
the mutant exhibits very low transport activity for rhodamine 6G compared to the wild type enzyme
E580K
-
the mutant exhibits partially impaired rhodamine 6G efflux functions
S1368A
-
the mutant has wild type enzyme levels as well as wild type ATPase activity and transmembrane signaling
S558Y
-
the mutation leads to markedly increased hypersensitivity towards all transport substrates
V656A
-
the mutation leads to markedly increased hypersensitivity towards all transport substrates
E574K
-
the mutant exhibits very low transport activity for rhodamine 6G compared to the wild type enzyme
-
E580K
-
the mutant exhibits partially impaired rhodamine 6G efflux functions
-
D25A
the mutation reduces the transport activity of the enzyme. The mutant retains its capacity to bind substrate, albeit at a lower level compared to the wild type
D25E
the mutation does not affect the transport function of the enzyme
R111A
the mutation results in a decrease in secondary structure content of the transporter
R111K
the mutation completely destabilizes the structure of the transporter
Q521A
-
the mutant of subunit PatA is similarly active as the wild type enzyme
E165Q
G44A
the mutant shows strongly reduced activity (less than 10%) compared to the wild type enzyme
G44S
the mutant shows strongly reduced activity (less than 10%) compared to the wild type enzyme
K47M
-
the mutation exhibits no doxorubicin efflux compared to the wild type enzyme
K47R
Q197H
Q197H/Y198H
the mutant shows strongly reduced activity (less than 10%) compared to the wild type enzyme
Q197H/Y198R
the mutant shows about 35% activity compared to the wild type enzyme
S141R
the mutant shows strongly reduced activity (less than 10%) compared to the wild type enzyme
S23C
-
the mutation has a slight decreasing effect on doxorubicin efflux compared to the wild type enzyme
S319C
-
the mutation has a slight decreasing effect on doxorubicin efflux compared to the wild type enzyme
Y18A
-
the mutation exhibits no doxorubicin efflux compared to the wild type enzyme
Y198R
the mutant shows about 30% activity (less than 10%) compared to the wild type enzyme
Y89C
-
the mutation has no effect on doxorubicin efflux compared to the wild type enzyme
D36N
-
the mutant shows no Na+ coupling and loss in H+ coupling compared to the wild type enzyme
D371N
-
the mutant shows loss in H+ coupling compared to the wild type enzyme
Q278A
-
the mutant shows no Na+ coupling and loss in H+ coupling compared to the wild type enzyme
additional information
K380R
-
mutation in the Walker A motif, deficient in ATPase activity and Hoechst 33342 transport
K380R
-
site-directed mutagenesis, the ATPase activity of the mutant is highly reduced
D34A/I239T/G354E
the mutations abolish the ability to confer n-dodecyl-N,N-dimethylamine N-oxide resistance to Escherichia coli
Y440F
-
MRP1 mutant, substitution of Tyr440 with Phe, as found in MRP3, reduces leukotriene C4 and GSH-stimulated estrone-3-sulfate transport without affecting transport of other substrates. The mutation increased the Km for LTC4 5fold and substantially reduces photolabeling of MRP1 by both LTC4 and the GSH derivative, azidophenacyl-GSH
Y440F
-
the mutant shows reduced activity with vincristine, VP-16, and doxorubicin compared to the wild-type enzyme
E165Q
the mutant shows strongly reduced activity (less than 10%) compared to the wild type enzyme
E165Q
-
the mutation shows 3% doxorubicin efflux compared to the wild type enzyme
K47R
the mutant shows strongly reduced activity (less than 10%) compared to the wild type enzyme
K47R
-
the mutation shows 24% doxorubicin efflux compared to the wild type enzyme
Q197H
the mutant shows strongly reduced activity (less than 20%) compared to the wild type enzyme
Q197H
-
the mutation shows 15% doxorubicin efflux compared to the wild type enzyme
additional information
-
a yvcC knockout mutant shows a lower rate of ethidium bromide efflux than the wild-type strain
additional information
-
substrate specificities of transmembrane segment mutants, overview
additional information
-
a cysteine-less green fluorescent protein-tagged variant of the enzyme is non-functional while the ATPase activity of the cysteine-less enzyme-His-expressing cells is 60% of that of the cells expressing wild type enzyme
additional information
-
co-expression of isoforms ABCG5 and ABCG8 in insect cells results in presence of a vanadate-sensitive ATPase activity in the membrane
additional information
-
construction of a series of MRP1/MRP3 hybrids. Substitution of the region encompassing transmembrane helices 8 and 9 and portions of cytoplasmic loops 4 and 5 of MRP1 with the equivalent region of MRP3 eliminates LTC4 transport
additional information
-
construction of a series of single cysteine isoforms of ABCB1, selection of mutations based on a direct comparison of the sequences of TM6 and TM12 and by inspection of our Sav1866-directed homology model of human ABCB1. 11 single cysteine isoforms generated provide both a longitudinal and rotational coverage of the alpha helix. Introduction of cysteine residues can affect the ATP binding, overview
additional information
-
introduction of cysteine residues into regions of TM3, residues 175-178, and TM9, residues 820822, that extend into the cytoplasm and are 4 A and 20 A apart in the closed and open conformations, respectively. Cross-linking of the double mutants with a short cross-linker, 1,1-methanediyl bismethanethiosulfonate at 0°C results only in cross-linking of mutant L175C/N820C
additional information
-
residues F368 and W995 do not play an important role in the initial binding of substrates
additional information
introduction of L1260A processing mutation in wild-type P-gp containing a C-terminal A52 epitope tag. Cysteine mutations A80C and R741C are introduced into the A52-tagged human Cys-less Pgp cDNA. In transmembrane segments 4-6 or 10-12, single cysteine mutations are introduced at positions K213-A233 (TM4), T294-Y316 (TM5), Q330-P350 (TM6), W855-E875 (TM10), H936-F957 (TM11), or V974-F994 (TM12)
additional information
-
introduction of L1260A processing mutation in wild-type P-gp containing a C-terminal A52 epitope tag. Cysteine mutations A80C and R741C are introduced into the A52-tagged human Cys-less Pgp cDNA. In transmembrane segments 4-6 or 10-12, single cysteine mutations are introduced at positions K213-A233 (TM4), T294-Y316 (TM5), Q330-P350 (TM6), W855-E875 (TM10), H936-F957 (TM11), or V974-F994 (TM12)
additional information
-
cysteine-free mouse MDR3 P-glycoprotein (Pgp) is constructed by mutagenesis of the nine natural Cys to Ala. Yield, purity, ATPase activity, KM (MgATP), and stimulation of ATPase by verapamil are similar to wild-type mouse Ppg. After long-term storage at -70 °C (6 months), or incubation at 37 °C for up to 2h, it shows the same stability as wild type (as measured by retention of ATPase activity)
additional information
-
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
additional information
-
construction of a Mrp4-knockout mouse model with cell-type specific expression and subcellular localisation, overview
additional information
-
introduction of cysteine residues into Cys-less P-glycoprotein and cysteine-mediated cross-linking. For mutant A627C/S1276C, disulfide formation is with high efficiency and cross-linked P-glycoprotein retains 30-68% drug-stimulated ATPase activity compared with reduced or cysteine-less P-glycoprotein. Cysteine pairs K615C/S1276C and A627C/K1260C also form a disulfide, but to a lesser extent, and the cross-linked form of these two mutants have lower drug-stimulated ATPase activity
additional information
-
overexpression of Yor1p confers resistance to oligomycin, rhodamine 6G and rhodamine B to cells. A yor1 gene disruption mutant is hypersensitive to oligomycin and rhomdamine 6G
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
optimal pH for stabilizing the recombinant enzyme protein during purification is pH 6.5. hMDR1 remains monodispersed at a pH range of pH 5.5-pH 7.5. In contrast, at a lower pH such as pH 4.5, the protein is precipitated
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 37
-
the specific ATPase activity is completely diminished after 2 h at 37°C, but 75% of the ATPase activity remains after 24 h at 10°C
additional information
-
no effect of trypsin cleavage on the thermostability of P-gp
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cholesterol hemisuccinate alters the thermal unfolding of the enzyme and greatly stabilizes its basal ATPase activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 6 months, cysteine-free mutant shows the same stability as the wild-type enzyme
-
most suitable component for maintaining hMDR1 activity is PIPES, rather than citric acid, imidazole, MES, or MOPS. Optimal pH for stabilizing the recombinant enzyme protein during purification is pH 6.5. Addition of CHS preserves 90% of the activity at 25°C after 1 day, whereas little or no activity remains without CHS. The specific ATPase activity is completely diminished after 2 h at 37°C, but 75% of the ATPase activity remains after 24 h at 10°C
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anti-Flag M2 affinity agarose gel chromatography and Superdex 200 gel filtration
approach involving its specific recognition onto a functionalized lipid layer containing a Ni-NTA lipidand allowing the purification of His-ABCG2 in presence of all solubilized membrane components that might be involved in the stabilisation of native oligomers and without requiring any additional washing or concentration passages
-
cobalt affinity resin column chromatography, GST column chromatography, and Superdex 200 gel filtration
cysteine-free mouse MDR3 P-glycoprotein (Pgp) is constructed by mutagenesis of the nine natural Cys to Ala, expressed in Pichia pastoris and purified
-
HiTrap chelating column chromatography and Superdex 200 gel filtration, in the presence of trans-4-(trans-4'-propylcyclohexyl)cyclohexyl-alpha-D-maltoside
-
immobilized metal ion affinity chromatography and Superdex 200 gel filtration
native enzyme from liver partially by mitochondria, plasma, endoplasmic reticulum and nuclear membrane fragment preparation
-
native P-gp by CHAPS-mediated extraction from plasma membrane, followed by concanavalin A affinity chromatography. Reconstitution in lipid proteoliposomes, that are further purified by gel filtration
-
Ni-NTA column chromatography
Ni-NTA column chromatography and Superdex 200 gel filtration
Ni-NTA resin column chromatography and Superdex 200 gel filtration
nickel affinity column chromatography and Superdex 200 gel filtration
recombinant His-tagged ABCB1 from Trichoplusia ni high-five cells by metal affinity chromatography
-
recombinant His10-tagged MDR1 249fold by metal chelate affinity chromatography and gel filtration, method optimization and evaluation
-
recombinant His10-tagged P-gp from BHK cells by nickel affinity chromatography
-
recombinant protein, reconstitution in proteoliposomes containing varying concentrations of cholesterol
-
recombinant wild-type and mutant enzymes from HEK-293 cells partially by membrane preparation
-
recombinant wild-type and mutant enzymes, reconstitution in proteoliposomes
-
TALON cobalt resin column chromatography, and Superdex 200 gel filtration
Ni-NTA resin column chromatography and Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination tissue and developmental expression patterns of genes Mdr1a, Mdr1b, and Mdr2, overview
-
expressed in Escherichia coli
expressed in Escherichia coli BL21[DE3]pLysS cells
expressed in Escherichia coli C41(DE3) cells
expressed in Escherichia coli DH5alpha cells
expressed in HEK-293 cells
expressed in Lactococcus lactis strain NZ9000
expressed in Pichia pastoris and Saccharomyces cerevisiae AD1-8u_ cells
expressed in Sf9 insect cells
expression in MDCK cell
expression in minicells of Escherichia coli, the bcrA bcrB and bcrC genes also confer resistance upon Escherichia coli
-
expression in Xenopus oocytes
expression of gene MDR1 in MDCK II cells, expression of His10-tagged P-gp in BHK cells
-
expression of His-tagged ABCB1 in Trichoplusia ni high-five cells using the baculovirus expression system
-
expression of His6-ABCG2 in Sf9 insect cells and in human Flp-In-293/ABCG2 cells
-
expression of P-glycoprotein or MRP1 in membranes from Trichoplusia ni High Five cells using the baculovirus transfection system, overexpression of P-glycoprotein in human carcinoma KB-C2 cells, overexpression of MRP1 in human KB/MRP cells
-
expression of the enzyme in L5178Y mouse T lymphoma parent cell line using the pHa MDR1/A retrovirus
-
expression of wild-type an dmutant N-terminal nucleotide binding domains in Escherichia coli strain BL21(DE3)
-
gene ABCB1 maps to chromosome 7q21.1, expression of MDR1 in L5178 mouse T-cell lymphoma cells
-
gene cdr1, overexpression in Saccharaomyces cerevisiae
gene MDR1, expression of wild-type and mutant MDR1571A enzymes in HEK-293 cells. MDR1 571 genotypes in leukemia patients, overview
gene Sav1866, sequence analysis and comparison with other ABC transporters
MDR1 gene expression in Sf9 cells, pgp1 gene overexpression in DC-3F/ADX cells
-
MDR1, large-scale expression of His10-tagged human MDR1 using a baculovirus/insect expressSF+ cell system
-
MRP2, DNA and amino acid sequence determination and analysis, expression of MRP2 in Spodoptera frugiperda Sf9 cells
-
MRP7 expression in HEK-293 cells, ectopic expression of MRP7 in mouse embryonic fibroblast deficient in P-glycoprotein and MRP1
-
native protein is expressed in Pichia pastoris strain SMD1163 and Sf9 insect cells, while selenomethionine-labeled protein is expressed in Hi5 cells
ORF1 and ORF2 are simultaneously required for an efficient induction of the multidrug resistance phenotype
-
overexpression of Cdr1p as a GFP-tagged protein in plasma membrane of Saccharomyces cerevisiae
-
overexpression of P-glycoprotein, MRP1, or BCRP in NIH-3T3 cells and in Leishmania tropica
-
P-glycoprotein overexpressionin NCI/ADR-RES and OVCAR-8 ovarian carcinoma cells
-
recombinant expression of His-tagged mutant enzymes in HEK 293 cells, recombinant expression of wild-type enzyme in Spodoptera frugiperda Sf9 cells
two forms of abcb1a are cloned from Sprague-Dawley cDNA that differ by six amino acids and a base pair deletion. The intact form is stably transfected in LLC-PK1 cells
-
wild-type human P-gp is expressed using the baculovirus/expressSF+ insect cell system
-
wild-type MRP1 and mutant hybrid MRP1/MRP3 are expressed in Sf21 insect cells as two half-molecules, comprising amino acids 1 to 932 and 932 to 1531, respectively, using the baculovirus expression vector, expression of wild-type and mutant MRP1 in HEK-293 cell membranes
-
ydaG and ydbA genes, separate expression in Lactococcus lactis NZ9000 using the nisin-inducible system
expressed in Escherichia coli C41(DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
erucin, glyceollins, soybean extract, sulforaphane, 5'-fluorouracil, bortezomib, bosentan, carbamazepine, cimetidine, cisplatin A, efavirenz, mitotane, obatoclax, pregnenolone-16alpha-carbonitrile, quinidine, saquinavirm spironolactone, vincristine, rifampicin, and tripanocide benznidazole induce enzyme mRNA expression
hepatocyte growth factor treatment increases the amount of enzyme on the cell surface in parallel with an increased transcription. Enzyme mRNA expression is also increased by epidermal growth factor, oxidative stress, phorbol ester, or activation of the aryl hydrocarbon receptor
-
high and specific P-glycoprotein transcript overexpression in PLHC-1/dox cells, about 160fold upregulation compared to PLHC-1/wt cells
-
p-glycoprotein and multidrug resistance-associated protein 2 protein expressions in liver are elevated after intake of hydrogen rich water
-
P-gp down-regulation by cyclooxygenase-2 inhibitors (indomethacin heptyl ester and nimesulide) can confer the diminution of drugs resistance, and consequently ameliorate the response to medical therapy in inflammatory bowel disease
-
resveratrol, 8-hydroxydaidzein. atorvastatin, epirubicin, ethanol, irinotecan, isopentanol, and topotecan downregulate enzyme mRNA expression
shikonin dose-dependently increases the protein and RNA expression of P-glycoprotein, multidrug resistance-associated protein 2/3, organic anion transporting polypeptides 1B1, and 2B1
-
the enzyme expression increases time-dependently (24 h: 130%; 48 h: 381%) after exposure to 0.006 mM 2,4,6-tribromophenol
-
the Mdr2 protein is not detected in livers from male and female rats at birth while mRNA is consistently expressed in livers at a high and steady level until 30 days of age
erucin, glyceollins, soybean extract, sulforaphane, 5'-fluorouracil, bortezomib, bosentan, carbamazepine, cimetidine, cisplatin A, efavirenz, mitotane, obatoclax, pregnenolone-16alpha-carbonitrile, quinidine, saquinavirm spironolactone, vincristine, rifampicin, and tripanocide benznidazole induce enzyme mRNA expression
erucin, glyceollins, soybean extract, sulforaphane, 5'-fluorouracil, bortezomib, bosentan, carbamazepine, cimetidine, cisplatin A, efavirenz, mitotane, obatoclax, pregnenolone-16alpha-carbonitrile, quinidine, saquinavirm spironolactone, vincristine, rifampicin, and tripanocide benznidazole induce enzyme mRNA expression
resveratrol, 8-hydroxydaidzein. atorvastatin, epirubicin, ethanol, irinotecan, isopentanol, and topotecan downregulate enzyme mRNA expression
resveratrol, 8-hydroxydaidzein. atorvastatin, epirubicin, ethanol, irinotecan, isopentanol, and topotecan downregulate enzyme mRNA expression
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of purified recombinant protein in proteoliposomes containing varying concentrations of cholesterol
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biofuel production
diagnostics
-
in patients with neuroblastoma, increased MRP4 expression has prognostic value
drug development
-
MRP4 is a potential target for drug development, e.g. in the treatment of hyperuricaemia
medicine
pharmacology
analysis
-
use of in vitro transporter assays for analysis of the role of P-glycoprotein mediated efflux activity. The transwell assay is a valuable tool to evaluate P-glycoprotein interaction with compounds for assessing brain penetration of new chemical entities
analysis
-
evaluation of high-speed ATPase activity assay method by comparing with in vitro transport assay systems using MDR1-transfected MDR1-MDCK cells. The kinetic parameters obtained in ATPase activity assay are not necessarily corresponding with those in in vitro transport assay. The combination of the ATPase activity assay and in vitro transport technologies gives insight into mechanisms
analysis
-
use of pharmacophore models for the prediction of binding to P-glycoprotein
analysis
-
use of in vitro transporter assays for analysis of the role of P-glycoprotein mediated efflux activity. The transwell assay is a valuable tool to evaluate human P-glycoprotein interaction with compounds for assessing brain penetration of new chemical entities
biofuel production
-
gene overexpression in industrial yeast strains improves the alcoholic fermentation performance for sustainable bio-ethanol production
biofuel production
-
gene overexpression in industrial yeast strains improves the alcoholic fermentation performance for sustainable bio-ethanol production
-
medicine
-
ATP-driven pumping of a variety of drugs out of cells by P-glycoprotein poses a serious problem to medical therapy
medicine
-
Pgp plays a central role in compromising cancer chemotherapy and in modulating the bioavailability and distribution of therapeutic agents
medicine
-
specific inhibitors of MRP4 can be a valuable asset for enhancing the brain penetration and therapeutic efficacy of adefovir and tenofovir
medicine
-
the presence of P-gp in various drug-resistant cancer cells can cause failure in chemotherapy, as it is able to transport a variety of anticancer drugs out of the cell
medicine
-
the direct inhibitory effects of indomethacin and SC236 on P-gp may contribute to their ability to increase the intracellular retention of doxorubicin and thus enhance its cytotoxicity. The combination of indomethacin or SC236 with doxorubicin may have significant potential clinical application, especially in the circumvention of P-gp-mediated multidrug resistance in cancer cells
medicine
-
rosemary phytochemicals, such as carnosic acid, have inhibitory effects on anticancer drug efflux transporter P-glycoprotein and may become useful to enhance the efficacy of cancer chemotherapy
medicine
-
procyanidine is a potent inhibitor of P-glycoprotein on blood-brain barrier and can improve the therapeutic effects on cerebral tumors of some drugs which are difficult to accumulate in the brain
medicine
-
development of a method for predicting the risk of drug-drug interactions involving inhibition of P-glycoprotein
medicine
-
lovastatin increases the absorption of verapamil (used as an antiarrhythmic agent to control supraventricular tachyarrhythmias) by inhibiting P-glycoprotein
medicine
-
the human multidrug resistance transporter P-glycoprotein (P-gp) prevents the entry of compounds into the brain by an active efflux mechanism at the blood-brain barrier. In treatment of neurodegenerative diseases the development of new reversible inhibitors of P-gp is pertinent to overcome this problem. Design and synthesis of a crosslinked agent based on the Alzheimers disease treatment galantamine (Gal-2, bis[(4aS,6R,8aS)-3-methoxy-11-methyl-5,6,9,10,11,12-hexahydro-4aH-[1]benzofuro[3a,3,2-ef][2]benzazepin-6-yl] decanedioate) that inhibits P-gp-mediated efflux from cultured cells. Gal-2 inhibits the efflux of the fluorescent P-gp substrate rhodamine 123 in cancer cells that over-express P-gp. It inhibits the efflux of therapeutic substrates of P-gp, such as doxorubicin, daunomycin and verapamil. Potential role of Gal-2, as inhibitors of P-gp at the blood-brain barrier to augment treatment of neurodegenerative diseases
pharmacology
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Cdr1p is a critical factor in the design of therapeutic strategies to combat antifungal resistance
pharmacology
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the investigation of the substrate interactions and modulation of multidrug transporters may pave the way for predictive toxicology and pharmacogenomics
EXTERNAL LINKS (specific for EC-Number 7.6.2.2)
Transporter Classification Database (TCDB): 3.A.1.208.43, 3.A.1.204.2, 9.A.1.1.1, 3.A.1.208.21, 3.A.1.106.13, 3.A.1.208.5, 3.A.1.201.24, 3.A.1.208.8, 3.A.1.208.2, 3.A.1.201.31, 3.A.1.208.6, 3.A.1.201.4, 3.A.1.201.1, 3.A.1.208.17, 3.A.1.201.13, 3.A.1.209.4, 3.A.1.208.20, 3.A.1.117.1, 3.A.1.208.9, 3.A.1.208.7, 3.A.1.208.15, 3.A.1.208.31, 3.A.1.208.13, 3.A.1.211.5, 3.A.1.201.14, 3.A.1.208.47, 3.A.1.204.15
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Release 2026.1 (March 2026)
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