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Information on EC 7.6.2.2 - ABC-type xenobiotic transporter and Organism(s) Caenorhabditis elegans and UniProt Accession P34712

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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).
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Caenorhabditis elegans
UNIPROT: P34712
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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ATP
+
H2O
+
xenobiotic[side 1]
=
ADP
+
phosphate
+
xenobiotic[side 2]
+
+
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP phosphohydrolase (xenobiotic-exporting)
-
-
-
-
MRP
-
-
-
-
multidrug-resistance protein
-
-
-
-
P-glycoprotein
-
-
-
-
Pgp
-
-
-
-
transporter protein MRP
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-
-
-
xenobiotic-transporting ATPase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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).
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + actinomycin D/in
ADP + phosphate + actinomycin D/out
show the reaction diagram
-
-
-
?
ATP + H2O + paclitaxel/in
ADP + phosphate + paclitaxel/out
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
vanadate
complete inhibition at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
actinomycin D
1 mM increases the ATPase activity of the enzyme more than 5times
dipyridamole
1 mM increases the ATPase activity of the enzyme more than 5times
paclitaxel
1 mM increases the ATPase activity of the enzyme more than 5times
progesterone
1 mM increases the ATPase activity of the enzyme more than 5times
valinomycin
1 mM increases the ATPase activity of the enzyme more than 5times
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGP1_CAEEL
1321
11
145063
Swiss-Prot
other Location (Reliability: 5)
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cobalt affinity resin column chromatography, GST column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
native protein is expressed in Pichia pastoris strain SMD1163 and Sf9 insect cells, while selenomethionine-labeled protein is expressed in Hi5 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Van Veen, H.W.; Konings, W.N.
The ABC family of multidrug transporters in microorganisms
Biochim. Biophys. Acta
1365
31-36
1998
Bacillus subtilis, Saccharomyces cerevisiae, Caenorhabditis elegans, Candida albicans, Cricetulus griseus, Escherichia coli, Entamoeba histolytica, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Levilactobacillus brevis, Lactococcus lactis, Leishmania donovani, Leishmania tarentolae, Staphylococcus aureus, Mycoplasma genitalium, Plasmodium falciparum
Manually annotated by BRENDA team
Jin, M.S.; Oldham, M.L.; Zhang, Q.; Chen, J.
Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans
Nature
490
566-569
2012
Caenorhabditis elegans (P34712), Caenorhabditis elegans
Manually annotated by BRENDA team