Information on EC 3.6.1.3 - adenosinetriphosphatase and Organism(s) Homo sapiens

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The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.1.3
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RECOMMENDED NAME
GeneOntology No.
adenosinetriphosphatase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
purine metabolism
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Purine metabolism
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase
Many enzymes previously listed under this number are now listed separately under EC 3.6.3 and EC 3.6.4.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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role for cell surface F1-adenosine triphosphatase in T cell activation by tumors and specific interactions between Vgamma9Vdelta2 TCRs and purified F1-ATPase. Contact of T cells with F1-ATPase on polystyrene beads can partially replace the cell-cell contact stimulus during phosphoantigen responses
additional information
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zoledronate treatment promotes F1-expression as well as endogenous phosphoantigen production. Recognition of phosphoantigens on cell membranes in the form of nucleotide derivatives that can bind to F1-ATPase acting as a presentation molecule
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
ADP + phosphate
show the reaction diagram
additional information
?
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the chromodomain helicase/adenosine triphosphatase DNA binding protein 1-like gene, encoding the enzyme, is a possible oncogene responsible for development of hepatocellular carcinomas by inhibition of apoptosis in the cells, molecular mechanism of CHD1L in hepatocarcinogenesis, overview. Interaction of CHD1L and Nur77 inhibits the nucleus-to-mitochondria translocation of Nur77, a critical member of a p53-independent apoptotic pathway, and the subsequent apoptotic pathway
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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
ADP + phosphate
show the reaction diagram
additional information
?
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the chromodomain helicase/adenosine triphosphatase DNA binding protein 1-like gene, encoding the enzyme, is a possible oncogene responsible for development of hepatocellular carcinomas by inhibition of apoptosis in the cells, molecular mechanism of CHD1L in hepatocarcinogenesis, overview. Interaction of CHD1L and Nur77 inhibits the nucleus-to-mitochondria translocation of Nur77, a critical member of a p53-independent apoptotic pathway, and the subsequent apoptotic pathway
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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protease La is an ATP-dependent protease, it requires ATP hydrolysis to digest larger, intact proteins, but can cleave small, fluorogenic peptides such as Glu-Ala-Ala-Phe-MNA by only binding, but not hydrolyzing, ATP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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substrate inhibition of wild-type and mutant enzymes, kinetics, overview
etretinate
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retinoic acid
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SDS
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inactivation of the enzyme at 12% SDS
additional information
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partial digestion with trypsin produces four fragments, 170 and 150 kDa and subsequently 125 and 110 kDa, which are recognized by anti-ABCA1 extracellular domain 1 antibody KM3073, and two fragments, 170 and 120 kDa, which are recognized by anti-ABCA1 NBF2 antibody
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
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triphosphoric acid 1-adenosin-5'-yl ester 3-(3-methylbut-3-enyl) ester
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an adenylated derivative of isopentenyl diphosphate, can stably bind to F1-ATPase-coated beads and promotes TCR aggregation, lymphokine secretion, and activation of the cytolytic process provided that nucleotide diphosphatase activity is present. It also acts as an allosteric activator of F1-ATPase
additional information
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both ATPase and peptidase activities can be stimulated by the binding of a larger protein substrate, such as beta-casein
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 1.2
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 0.059
ATP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.15
ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.001
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below, purified recombinant mutant K939M/K1952M enzyme
0.5
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above, purified recombinant wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
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assay at
7.5
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assay at
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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activated by phosphoantigens provided exogenously or produced by tumors and infected cells. Activation requires a contact between Vgamma9Vdelta2 cells and neighboring cells, F1-ATPase is required for the response to inosine diphosphate
Manually annotated by BRENDA team
additional information
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three MHC-I-deficient 721.221 cell lines do not express surface F1-ATPase
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method, using 0.2 M magnesium chloride, 0.1 M Bis-Tris, 25% (w/v) PEG-3350, ADP and MgCl2 at pH 5.5 and 4°C (isoform HSPA1A), or 0.2 M trimethyl amine n-oxide, 0.1 M Tris, 26% (w/v) PEG monomethyl ether-2000, ADP and MnCl2, at pH 8.5 and 4°C (isoform HSPA1L), or 0.2 M ammonium acetate, 0.1M Bis-Tris, 25% (w/v) PEG-3350, ADP and MgCl2, at pH 5.5 and 4°C (isoform HSPA2), or 0.2 M calcium chloride, 0.1 M sodium acetate, 20% (w/v) PEG-6000, ADP and MgCl2, at pH 5.0 and 20°C (isoform HSPA5), or 0.1M disodium hydrogen phosphate, 0.1 M citric acid, 16% (w/v) PEG-300, ADP and MgCl2, at pH 3.2 and 20°C (isoform HSPA6)
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap chelating column chromatography and Superdex-200 gel filtration
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recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography and gel filtration
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recombinant wild-type and mutant His-tagged ABCA1s from insect Sf9 cell microsomal membranes by nickel affinity and anion exchange chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of gene CHD1L, previously called ALC1, within the 1q21 amplicon, by hybrid selection using microdissected DNA from chromosome 1q21
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expressed in Escherichia coli BL21(DE3)R3 pRARE cells
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expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta 2 (DE3)
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stable expression of ABCA1 in human fibroblasts WI-38 and HEK-293 cell membranes, expression of His-tagged wild-type and mutant ABCA1s in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G893A
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site-directed mutagenesis, the mutant shows 63% of wild-type ATPase activity, 80% of wild-type protease activity, and 2.27fold of the activation by beta-casein compared to the wild-type enzyme
G893A/G894A
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site-directed mutagenesis, the mutant shows 103% of wild-type ATPase activity, 79% of wild-type protease activity, and 0.745fold of the activation by beta-casein compared to the wild-type enzyme
G893A/G894P
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site-directed mutagenesis, the mutant shows 112% of wild-type ATPase activity, no protease activity, and 0.32fold of the activation by beta-casein compared to the wild-type enzyme
G893P
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site-directed mutagenesis, the mutant shows 89% of wild-type ATPase activity, no protease activity, and 0.49fold of the activation by beta-casein compared to the wild-type enzyme
G893P/G894A
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site-directed mutagenesis, the mutant shows 71% of wild-type ATPase activity, 8% of wild-type protease activity, and 0.23fold of the activation by beta-casein compared to the wild-type enzyme
G894A
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site-directed mutagenesis, the mutant shows 139% of wild-type ATPase activity, 76% of wild-type protease activity, and 0.49fold of the activation by beta-casein compared to the wild-type enzyme
G894P
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site-directed mutagenesis, the mutant shows 130% of wild-type ATPase activity, 84% of wild-type protease activity, and 0.23fold of the activation by beta-casein compared to the wild-type enzyme
G894S
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site-directed mutagenesis, the mutant shows 140% of wild-type ATPase activity, 47% of wild-type protease activity, and 0.88fold of the activation by beta-casein compared to the wild-type enzyme
K529R
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site-directed mutagenesis, inactive mutant
K939M/K1952M
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site-directed mutagenesis of Walker A motif residues, the mutant shows highly reduced activity compared to the wild-type enzyme
S855A
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site-directed mutagenesis, the mutant shows 78% of wild-type ATPase activity, no protease activity, and 0.35fold of the activation by beta-casein compared to the wild-type enzyme
T880V
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site-directed mutagenesis, the mutant shows 46% of wild-type ATPase activity, 107% of wild-type protease activity, and 3.28fold of the activation by beta-casein compared to the wild-type enzyme
W770A
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site-directed mutagenesis, the mutant shows 98.5% of wild-type ATPase activity, 6.4% of wild-type protease activity, and 0.305fold of the activation by beta-casein compared to the wild-type enzyme
W770P
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site-directed mutagenesis, the mutant shows 123% of wild-type ATPase activity, 55.3% of wild-type protease activity, and 0.64fold of the activation by beta-casein compared to the wild-type enzyme
additional information
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a CHD1L ubiquitous expression transgenic mouse model shows spontaneous tumor formation 24.4% of transgenic mice with the formation of heptaocellular carcinoma in four mice, but not in their 39 wild-type littermates, overview. Silencing CHD1L expression by siRNA restores staurosporine-induced apoptosis
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution of purified recombinant enzyme in lipid vesicles consisting of L-alpha-lecitin from soybean, sphingomyelin, synthesized phospholipids, or sterols, in 40 mM Tris-HCl, pH 7.5, 0.1 mM EGTA, overview
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