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Information on EC 3.6.1.5 - apyrase and Organism(s) Rattus norvegicus and UniProt Accession Q5DRK1
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3.6.1.5 apyraseIUBMB Comments
Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
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Word Map
- 3.6.1.5
- platelet
-
purinergic
- agonist
- endothelial
- suramin
- ntpdases
- 5'-nucleotidase
- thrombin
- utp
- fibrinogen
-
thromboxane
-
salivary
-
blocker
- ecto-nucleotidases
-
ecto-5\'-nucleotidase
-
purinoceptors
-
platelet-rich
- aspirin
- 5'-triphosphate
-
ecto-enzymes
- ouabain
-
ppads
- oligomycin
-
adp-induced
-
synaptosomes
- serca2
- hirudin
-
blood-feeding
-
atp-mediated
- carbenoxolone
-
tyrode
-
hemichannels
-
alpha,beta-methylene
- arl
-
pannexins
-
atp-hydrolyzing
- luciferin-luciferase
-
adenosinergic
- agriculture
-
e-type
- phlebotomus
- analysis
- pharmacology
-
hematophagous
-
adp-dependent
- medicine
-
preretinal
-
gel-filtered
- ap5a
-
aggregometry
-
bzatp
- drug development
-
ectonucleotide
-
3.1.3.5
- atpgammas
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
apyrase, ecto-atpase, adpase, ntpdase3, atp diphosphohydrolase, entpd1, atpase 2, ecto-apyrase, ectonucleoside triphosphate diphosphohydrolase, atpdase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine diphosphatase
-
-
-
-
ADPase
-
-
-
-
ATP-diphosphatase
-
-
-
-
ATP-diphosphohydrolase
-
-
-
-
ATPDase
-
-
-
-
CD39 antigen
-
-
-
-
Golgi nucleoside diphosphatase
-
-
-
-
HB6
-
-
-
-
Lymphoid cell activation antigen
-
-
-
-
NTPDase1
NTPDase3
-
-
-
-
nucleoside triphosphate diphosphohydrolase
NTPDase1
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside triphosphate phosphohydrolase (nucleoside monophosphoate-forming)
Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
CAS REGISTRY NUMBER
COMMENTARY
9000-95-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2 H2O
AMP + 2 phosphate
sequential dephosphorylation of ATP to ADP and then AMP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
salvage of purine nucleobases in primary urine
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
regulation of extracellular ATP-level
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
ATP and ADP are hydrolyzed equivalently
-
-
?
ATP + H2O
ADP + phosphate
ATP incubated with NTPDase2 is readily converted into ADP, but very poorly into AMP
-
-
?
additional information
?
-
-
both ATP and ADP hydrolysis occur at the same active site of enzyme
-
-
?
additional information
?
-
-
enzyme is involved in regulating ATP signaling associated primarily with auditory neurotransmission
-
-
?
additional information
?
-
establishment of a kinetic isothermal titration calorimetry assay. Substrate recognition by NTPDase1, overview
-
-
?
additional information
?
-
production of inorganic phosphate is measured using the malachite green method
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme is involved in regulating ATP signaling associated primarily with auditory neurotransmission
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
salvage of purine nucleobases in primary urine
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
regulation of extracellular ATP-level
-
-
?
ATP + H2O
ADP + phosphate
ATP incubated with NTPDase2 is readily converted into ADP, but very poorly into AMP
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
Cl-
the active-site clefts of NTPDase1 contain three chloride ions, one of which is bound to the second phosphate-binding loop, apyrase conserved region 4, ACR4
Mg2+
additional information
complex structures with decavanadate and heptamolybdate show that both polyoxometallates bind electrostatically to a loop that is involved in binding of the nucleobase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3,5-dimethyl-1H-pyrazol-1-yl) (m-tolyl)methanone
-
(3,5-dimethyl-1H-pyrazol-1-yl) (naphthalen-2-yl)methanone
-
(3,5-dimethyl-1H-pyrazol-1-yl) (o-tolyl)methanone
-
(3,5-dimethyl-1H-pyrazol-1-yl) (pyridin-4-yl)methanone
-
(4-aminophenyl) (3,5-dimethyl-1H-pyrazol-1-yl)methanone
-
(4-aminophenyl) (3,5-dimethyl-4-(p-tolyloxy)-1H-pyrazol-1-yl)methanone
-
(4-aminophenyl) (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (4-chlorophenyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (m-tolyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (naphthalen-2-yl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (o-tolyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (p-tolyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (pyridin-4-yl)methanone
-
(4-chlorophenyl) (3,5-dimethyl-1H-pyrazol-1-yl)methanone
-
(4-chlorophenyl) (3,5-dimethyl-4-(p-tolyloxy)-1H-pyrazol-1-yl)methanone
-
(E)-1-(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl)-3-phenylprop-2-en-1-one
-
(R)-1-(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl)-2-(4-isobutylphenyl)propan-1-one
-
1-(4-aminobenzoyl)-5-methyl-1H-pyrazol-3(2H)-one
-
1-amino-4-[(naphthalen-1-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
-
3,5-dimethyl-4-(naphthalen-2-yloxy)-1H-pyrazole
-
3-methyl-2-(4-methylbenzoyl)-1,2-dihydropyrazol-5-one
-
(3,5-dimethyl-1H-pyrazol-1-yl) (m-tolyl)methanone
-
(3,5-dimethyl-1H-pyrazol-1-yl) (naphthalen-2-yl)methanone
-
(3,5-dimethyl-1H-pyrazol-1-yl) (o-tolyl)methanone
-
(3,5-dimethyl-1H-pyrazol-1-yl) (pyridin-4-yl)methanone
-
(4-aminophenyl) (3,5-dimethyl-1H-pyrazol-1-yl)methanone
-
(4-aminophenyl) (3,5-dimethyl-4-(p-tolyloxy)-1H-pyrazol-1-yl)methanone
-
(4-aminophenyl) (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (4-chlorophenyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (m-tolyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (naphthalen-2-yl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (o-tolyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (p-tolyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (pyridin-4-yl)methanone
-
(4-chlorophenyl) (3,5-dimethyl-1H-pyrazol-1-yl)methanone
-
(4-chlorophenyl) (3,5-dimethyl-4-(p-tolyloxy)-1H-pyrazol-1-yl)methanone
-
(E)-1-(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl)-3-phenylprop-2-en-1-one
-
(R)-1-(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl)-2-(4-isobutylphenyl)propan-1-one
-
1-(4-aminobenzoyl)-5-methyl-1H-pyrazol-3(2H)-one
-
3,5-dimethyl-4-(naphthalen-2-yloxy)-1H-pyrazole
-
3-methyl-2-(4-methylbenzoyl)-1,2-dihydropyrazol-5-one
-
ADP
-
hydrolysis of CaATP2- and CaADP- decreased by 50% at 0.48 mM free ADP
Sodium azide
-
not inhibitory at 1 mM, 25% inhibition of ATPase activity at 20 mM
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
-
no inhibition by P1,P5-di(adenosine-5'-)pentanphospate
-
additional information
-
not inhibitory: oligomycin, ouabain, bafilomycin A, theophylline, thapsigarin, ethacrynic acid, P1,P5-(adenosine-5)pentyphosphate, omeprazole
-
additional information
-
not inhibitory: ouabain, N-ethylmaleimide, lanthanum, oligomycin, levamisole, cAMP
-
additional information
inhibition mechanism of polyoxometallates, overview
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-glutamate
-
activation of ATP hydrolysis, no activation of ADP hydrolysis
tri-iodothyronine
-
increase in enzyme activity and enzyme mRNA in isolated myocytes
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0131
GDP
in presence of 0.1 mM UMP, recombinant wild-type enzyme, pH 7.4, 25°C
0.0488
GDP
in presence of 0.1 mM AMP, recombinant wild-type enzyme, pH 7.4, 25°C
0.149
GDP
in presence of 0.1 mM AHM, recombinant wild-type enzyme, pH 7.4, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
82.6
GDP
in presence of 0.1 mM AMP, recombinant wild-type enzyme, pH 7.4, 25°C
83.2
GDP
in presence of 0.1 mM UMP, recombinant wild-type enzyme, pH 7.4, 25°C
103.7
GDP
in presence of 0.1 mM AHM, recombinant wild-type enzyme, pH 7.4, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
700
GDP
in presence of 0.1 mM AHM, recombinant wild-type enzyme, pH 7.4, 25°C
1700
GDP
in presence of 0.1 mM AMP, recombinant wild-type enzyme, pH 7.4, 25°C
6400
GDP
in presence of 0.1 mM UMP, recombinant wild-type enzyme, pH 7.4, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00859
ammonium heptamolybdate
recombinant wild-type enzyme, pH 7.4, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
restricted to the canalicular membrane domain of hepatocytes
expression of isozymes NTPDase1, -2, and -8 in distinct liver compartments in normal and fibrotic rat liver
-
substantial portion of ATP-hydrolyzing activity depends on enzyme, enzyme is coexpressed with ecto-ATPase
-
increase in enzymic activity from birth to day 30, decrease afterwards, highest enzymic activity at day 30, highest affinity for enzyme at day 365, relative abundance of enzyme is highest at day 15 of ontogeny
-
marked enzyme immunoreactivity in primary afferent neurones of the spiral ganglion and synaptic regions of the inner and outer hair cells
expression of isozymes NTPDase1, -2, and -8 in distinct liver compartments in normal and fibrotic rat liver
additional information
-
immunoreactive enzyme detected exclusively in neurons, primarily in axon-like structures and presynaptic elements. No enzyme in noradrenaline cells or terminals. Enzyme immunopositive cells mostly also express hypocretin-1/orexin-A
-
substantial portion of ATP-hydrolyzing activity depends on enzyme, enzyme is coexpressed with ecto-ATPase
additional information
enzyme tissue localization by in situ immunohistochemistry, overview
additional information
enzyme tissue localization by in situ immunohistochemistry, overview
additional information
enzyme tissue localization by in situ immunohistochemistry, overview
additional information
enzyme tissue localization by in situ immunohistochemistry, overview
additional information
enzyme tissue localization by in situ immunohistochemistry, overview
additional information
enzyme tissue localization by in situ immunohistochemistry, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
metabolism
plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
physiological function
additional information
influence of transmembrane helix dynamics on activity is achieved by coupling to a domain motion. Active site structure of NTPDase1, overview, closure movement in NTPDases
physiological function
nucleoside triphosphate diphosphohydrolases are a physiologically important class of membrane-bound ectonucleotidases responsible for the regulation of extracellular levels of nucleotides
physiological function
the enzyme blocks platelet aggregation and supports blood flow
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ENTP8_RAT
494
2
54330
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
-
crosslinking experiments with glutaraldehyde plus SDS-PAGE, or blue native PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
detection of bands of 95000, 80000, 60000 Da by antibody
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
treatment with endoH or PNGase F results in a protein of 56000 Da
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
NTPDase1 that lacks the two transmembrane helices and an additional putative membrane interaction loop, hanging drop vapor diffusion method, using 0.1 M sodium acetate (pH 4.5), 3.6 M sodium chloride
purified recombinant wild-type enzyme, free or in complex with decavanadate or heptamolybdate, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of chimeric proteins from enzyme and ectoATPase. ectoATPase prefers ATP as substrate over ADP and releases mainly ADP. Chimeras contain N-terminal sequences of enzyme of increasing length fused to ectoATPase and vice versa. Protein structure rather than conserved regions may be of major relevance for determining differences in the catalytic properties
additional information
replacement of the extracellular domain of Rattus norvegicus NTPDase1, i.e. amino acid sequence 190TQEQSWLNFISDSQKQA206, with the shorter hydrophilic loop found in Homo sapiens NTPDase6, 240KTPGGS245. This NTPDase1 ECD DELTAMIL mutant variant is a soluble NTPDase1 that lacks a putative membrane interaction loop identified between the two lobes of the catalytic domain
additional information
efficient PiggyBac-mediated transposition of the recombinant soluble enzymes, method overview. Transfected cells secrete an enzymatically active wild-type soluble NTPDase1/CD39
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the detergents Triton X-100, deoxycholate, CHAPS, Nonidet, N-octoglucoside, C12E8 inactivate the enzyme, digitonin is not harmful
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Entpd8, recombinant expression in COS-7 cells
gene Entpd1, recombinant expression in COS-7 cells
gene Entpd2, recombinant expression in COS-7 cells
gene Entpd3, recombinant expression in COS-7 cells
gene Entpdase1, the sequence is constructed comprising the rat coding sequence from Thr38 to Thr476, which removes the nucleotides coding for the hydrophobic regions at the N- and C-terminals, and fused to a sequence coding for the rat IL-2-derived leader sequence that allows the enzyme to be secreted. Donor constructs are driven by EF1A promoter. Stable recombinant expression of wild-type and mutant enzymes in C6 glioma cells by the non-viral transfection with transposon PiggyBac-based method, real-time PCR expression analysis, transfected cells secrete an enzymatically active wild-type soluble NTPDase1/CD39
recombinant expression of the mutant NTPDase1 ECD DELTAMIL in Escherichia coli in soluble form and refolding to the active state
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beaudoin, A.R.; Vachereau, A.; Grondin, G.; St-Jean, P.; Rosenberg, M.D.; Strobel, R.
Microvesicular secretion, a mode of cell secretion associated with the presence of an ATP-diphosphohydrolase
FEBS Lett.
203
1-2
1986
Rattus norvegicus
Heine, P.; Braun, N.; Heilbronn, A.; Zimmermann, H.
Functional characterization of rat ecto-ATPase and ecto-ATP diphosphohydrolase after heterologous expression in CHO cells
Eur. J. Biochem.
262
102-107
1999
Rattus norvegicus
De Oliveira, M.E.; Battastini, O.A.M.; Meirelles, M.N.; Moreira, M.C.; Dias, R.D.; Sarkis, J.J.
Characterization and localisation of an ATP diphosphohydrolase activity (EC 3.6.1.5) in sarcolemmal membrane from rat heart
Mol. Cell. Biochem.
170
115-123
1997
Rattus norvegicus
Valenzuela, M.A; Ketttlun, A.M.; Sandoval, S.; Garcia, L.; Mancilla, M.; Neckelmann, G.; Chayet, L.; Alvarez, A.; Cuevas, F.; Collados, L.; Espinosa, V.; Traverso-Cori, A.; Bravo, I.; Acevedo, C.G.; Aranda, E.
Comparison of the biochemical properties, regulation and function of ATP diphosphohydrolase from human placenta and rat kidney
Braz. J. Med. Biol. Res.
29
589-597
1996
Homo sapiens, Rattus norvegicus
Battastini, A.M.O.; Oliveira, E.M.; Moreira, C.M.; Bonan, C.D; Sarkis, J.J; Dias, R.D.
Solubilization and characterization of an ATP diphosphohydrolase (EC 3.6.1.5) from rat brain synaptic plasma membranes
Biochem. Mol. Biol. Int.
37
209-219
1995
Rattus norvegicus
Frassetto, S.S.; Dias, R.D.; Sarkis, J.J.
Inhibition and kinetic alterations by excess free ATP and ADP of the ATP disphosphohydrolase activity (EC 3.6.1.5) from rat blood platelets
Biochem. Mol. Biol. Int.
35
499-506
1995
Rattus norvegicus
Frassetto, S.S.; Dias, R.D.; Sarkis, J.J.
Characterization of an ATP diphosphohydrolase activity (apyrase EC 3.6.1.5) in rat blood platelets
Mol. Cell. Biochem.
129
47-55
1993
Rattus norvegicus
Demenis, M.A.; Furriel, R.P.M.; Leone, F.A.
Characterization of an ectonucleoside triphosphate diphosphohydrolase 1 activity in alkaline phosphatase-depleted rat osseous plate membranes: possible functional involvement in the calcification process
Biochim. Biophys. Acta
1646
216-225
2003
Rattus norvegicus
Heine, P.; Braun, N.; Sevigny, J.; Robson, S.C.; Servos, J.; Zimmermann, H.
The C-terminal cysteine-rich region dictates specific catalytic properties in chimeras of the ectonucleotidases NTPDase1 and NTPDase2
Eur. J. Biochem.
268
364-373
2001
Rattus norvegicus
Failer, B.U.; Aschrafi, A.; Schmalzing, G.; Zimmermann, H.
Determination of native oligomeric state and substrate specificity of rat NTPDase1 and NTPDase2 after heterologous expression in Xenopus oocytes
Eur. J. Biochem.
270
1802-1809
2003
Rattus norvegicus
Bruno, A.N.; Bonan, C.D.; Wofchuk, S.T.; Sarkis, J.J.; Battastini, A.M.
ATP diphosphohydrolase (NTPDase 1) in rat hippocampal slices and effect of glutamate on the enzyme activity in different phases of development
Life Sci.
71
215-225
2002
Rattus norvegicus
Pierre Oses, J.; Cardoso, C.M.; Albuquerque Germano, R.; Barreto Kirst, I.; Rucker, B.; Ribas Furstenau, C.; Wink, M.R.; Bonan, C.D.; Oliveira Battastini, A.M.; Freitas Sarkis, J.J.
Soluble NTPDase: An additional system of nucleotide hydrolysis in rat blood serum
Life Sci.
74
3275-3284
2004
Rattus norvegicus
Boeck, C.R.; Sarkis, J.J.; Vendite, D.
Kinetic characterization and immunodetection of ecto-ATP diphosphohydrolase (EC 3.6.1.5) in cultured hippocampal neurons
Neurochem. Int.
40
449-453
2002
Rattus norvegicus
Nedeljkovic, N.; Banjac, A.; Horvat, A.; Stojiljkovic, M.; Nikezic, G.
Ecto-ATPase and ecto-ATP-diphosphohydrolase are co-localized in rat hippocampal and caudate nucleus synaptic plasma membranes
Physiol. Res.
52
797-804
2003
Rattus norvegicus
Henz, S.L.; Ribeiro, C.G.; Rosa, A.; Chiarelli, R.A.; Casali, E.A.; Sarkis, J.J.
Kinetic characterization of ATP diphosphohydrolase and 5'-nucleotidase activities in cells cultured from submandibular salivary glands of rats
Cell Biol. Int.
30
214-220
2006
Rattus norvegicus
Vlajkovic, S.M.; Vinayagamoorthy, A.; Thorne, P.R.; Robson, S.C.; Wang, C.J.; Housley, G.D.
Noise-induced up-regulation of NTPDase3 expression in the rat cochlea: Implications for auditory transmission and cochlear protection
Brain Res.
1104
55-63
2006
Rattus norvegicus
Nedeljkovic, N.; Banjac, A.; Horvat, A.; Stojiljkovic, M.; Nikezic, G.
Developmental profile of NTPDase activity in synaptic plasma membranes isolated from rat cerebral cortex
Int. J. Dev. Neurosci.
23
45-51
2005
Rattus norvegicus
Barreto-Chaves, M.L.; Carneiro-Ramos, M.S.; Cotomacci, G.; Junior, M.B.; Sarkis, J.J.
E-NTPDase 3 (ATP diphosphohydrolase) from cardiomyocytes, activity and expression are modulated by thyroid hormone
Mol. Cell. Endocrinol.
251
49-55
2006
Rattus norvegicus
Belcher, S.M.; Zsarnovszky, A.; Crawford, P.A.; Hemani, H.; Spurling, L.; Kirley, T.L.
Immunolocalization of ecto-nucleoside triphosphate diphosphohydrolase 3 in rat brain: Implications for modulation of multiple homeostatic systems including feeding and sleep-wake behaviors
Neuroscience
137
1331-1346
2006
Rattus norvegicus
Fausther, M.; Lecka, J.; Soliman, E.; Kauffenstein, G.; Pelletier, J.; Sheung, N.; Dranoff, J.; Sevigny, J.
Coexpression of ecto-5'-nucleotidase/CD73 with specific NTPDases differentially regulates adenosine formation in the rat liver
Am. J. Physiol. Gastrointest. Liver Physiol.
302
447-459
2012
Rattus norvegicus (O35795), Rattus norvegicus (P97687), Rattus norvegicus (Q5DRK1), Rattus norvegicus Sprague-Dawley (O35795), Rattus norvegicus Sprague-Dawley (P97687), Rattus norvegicus Sprague-Dawley (Q5DRK1)
Zebisch, M.; Krauss, M.; Schaefer, P.; Straeter, N.
Crystallographic evidence for a domain motion in rat nucleoside triphosphate diphosphohydrolase (NTPDase) 1
J. Mol. Biol.
415
288-306
2012
Rattus norvegicus (P97687)
Zebisch, M.; Baqi, Y.; Schaefer, P.; Mueller, C.E.; Straeter, N.
Crystal structure of NTPDase2 in complex with the sulfoanthraquinone inhibitor PSB-071
J. Struct. Biol.
185
336-341
2014
Rattus norvegicus (O35795)
Beckenkamp, L.R.; Iser, I.C.; Onzi, G.R.; Fontoura, D.M.S.D.; Bertoni, A.P.S.; Sevigny, J.; Lenz, G.; Wink, M.R.
Characterization of soluble CD39 (SolCD39/NTPDase1) from PiggyBac nonviral system as a tool to control the nucleotides level
Biochem. J.
476
1637-1651
2019
Rattus norvegicus (P97687)
Channar, P.A.; Afzal, S.; Ejaz, S.A.; Saeed, A.; Larik, F.A.; Mahesar, P.A.; Lecka, J.; Sevigny, J.; Erben, M.F.; Iqbal, J.
Exploration of carboxy pyrazole derivatives synthesis, alkaline phosphatase, nucleotide pyrophosphatase/phosphodiesterase and nucleoside triphosphate diphosphohydrolase inhibition studies with potential anticancer profile
Eur. J. Med. Chem.
156
461-478
2018
Rattus norvegicus (O35795), Rattus norvegicus (P97687), Rattus norvegicus (Q5DRK1), Rattus norvegicus (Q80Z26)
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