Information on EC 3.6.3.11 - Cl--transporting ATPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.6.3.11
-
RECOMMENDED NAME
GeneOntology No.
Cl--transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Cl-/out = ADP + phosphate + Cl-/in
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
transmembrane transport
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (Cl--importing)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. An animal and plant enzyme involved in the import of chloride anions.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to the P-type transport ATPases
physiological function
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the enzyme plays a role as Cl- channel and coupled to GABAA receptors. It might also play a role in anion transport across the neuronal membrane is required to evaluate the pathogenesis of some diseases, e.g. epilepsy
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 + Cl-/out
ADP + phosphate + Cl-/in
show the reaction diagram
Br-/out + ATP + H2O
Br-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
F-/out + ATP + H2O
F-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Cl-/out
ADP + phosphate + Cl-/in
show the reaction diagram
Br-/out + ATP + H2O
Br-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
F-/out + ATP + H2O
F-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
the enzyme acts as an ethacrynic acid-sensitive ATPase chloride pump in the central nervous system involved in regultion of postsynaptic membrane potentials, the raft protein NAP-22 might be involved in the regulation of ion transport through the membrane
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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
can substitute for Mg2+
Cl-
-
stimulates the dephosphorylation step
HCO3-
-
maximal activity in the presence of both anions at a Cl-/HCO3- in a ratio of 5:1 for Cl-,HCO3--ATPase
Mn2+
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can substitute for Mg2+
Zn2+
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can substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetazolamide
-
-
adenosine triphosphopyridoxal
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activity inhibited in a concentration-dependent fashion, IC 50 at 0.017 mM
bicuculline
-
-
Ethacrynic acid
N-ethylmaleimide
oligomycin
-
-
orthovanadate
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inhibitor of the transient-state phosphate bond
p-chloromercuribenzene sulfonate
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p-chloromercuribenzoate
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52% inhibition at 0.1 mM
Thiocyanate
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-
vanadate
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 2.6
ATP
7.4 - 10.3
Cl-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
adenosine triphosphopyridoxal
Acetabularia acetabulum
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activity inhibited in a concentration-dependent fashion, IC 50 at 0.017 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.46
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Cl-ATPase activity with 5 mM ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 7.8
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activity reduced at values below or above
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 42
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activity reduced or not detectable at values below or above
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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subcellular localization analysis, overview
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56290
CIP55 subunit, calculated from amino acid sequence, confirmed by SDS-PAGE
110000
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SDS-PAGE
300000
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SDS-PAGE
520000
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SDS-PAGE
580000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
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a,b,c subunit, 1 * 54000 + 1 * 50000 + 1 * 40000
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
subunit CIP55
phosphoprotein
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transient phosphorylation is the first step in the catalytic cycle, dephosphorylation occurs after Cl- transport
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at 4°C ATPase is released from liposomes it was incorporated in and loses the activity
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in the presence of liposomes: 80% loss of activity after 2 h at 4°C with freeze-thaw method, in the absence of liposomes: stable in Mono Q-III fraction, loss of activity after 24 h for all samples
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of the subunit CIP55 in Escherichia coli