Any feedback?
Information on EC 3.6.1.5 - apyrase and Organism(s) Solanum tuberosum and UniProt Accession P80595
for references in articles please use BRENDA:EC3.6.1.5Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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: Solanum tuberosum
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
-
-
-
-
additional information
-
apyrase belongs to the actin superfamily of proteins and is a member of the NTPDase family
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
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate + H2O
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-phosphate + phosphate
-
-
-
-
?
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate + H2O
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-phosphate + phosphate
-
-
-
-
?
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate + H2O
3'(2')-O-(methylanthranoyl)adenosine 5'-phosphate + phosphate
-
-
-
-
?
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate + H2O
3'(2')-O-(methylanthranoyl)adenosine 5'-phosphate + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
additional information
?
-
-
introduction of large groups in the ribose does not produce steric hindrance in substrate binding, but causes a reduction in kcat-value
-
-
?
additional information
?
-
-
apyrases hydrolyze nucleoside triphosphates and diphosphates
-
-
?
additional information
?
-
-
identification of the amino acids interacting with the nucleoside triphosphate substrate and probably involved in the catalyzed hydrolysis. The mixed two-step catalytic mechanism of hydrolysis involves Thr127 and Thr55 as potential nucleophilic factors responsible for the cleavage of the Pgamma and Pbeta anhydride bonds, respectively. Their is assisted by Glu170 and Glu78 residues, respectively, detailed overview
-
-
?
additional information
?
-
-
optimization of a luminescence-based high-throughput screening assay for detecting apyrase activity, overview
-
-
-
additional information
?
-
-
phosphate release 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
?
-
-
apyrases hydrolyze nucleoside triphosphates and diphosphates
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mg2+
-
an increase in ADPase activity in presence of Mg2+ ions occurs in case of isoform APY5
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
development of a high-throughput screening (HTS)-compatible format for inhibitor screening, a luminescence-based detection system as cost-effective biochemical assay in microplates, overview. 0.1% DMSO and 0.01% Tween 20 have no effect on enzyme stability and activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetic modeling of free and immobilized enzymes, overview
-
0.009
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
0.019
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
0.008
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
0.018
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
0.014
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
0.017
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
0.012
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
0.018
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
70
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
328
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
191
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
982
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
23
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
828
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
800
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
965
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.7
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6
7.2
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
apyrase decreases microglial ramification and surveillance. Applying the ATPase apyrase, an enzyme which hydrolyzes ATP and ADP, reduces microglial process ramification and surveillance in acutely prepared postnatal day (P)12 rat hippocampal slices, suggesting that ambient ATP/ADP maintains microglial surveillance. But attempting to raise the level of ATP/ADP by blocking the endogenous ecto-ATPase (termed NTPDase1/CD39), which also hydrolyzes ATP/ADP, does not affect the cells' ramification or surveillance, nor their membrane currents, which respond to even small rises of extracellular [ATP] or [ADP] with the activation of K+ channels. This indicates a lack of detectable ambient ATP/ADP and ecto-ATPase activity, contradicting the results with apyrase. Contamination of commercially available apyrase by a high K+ concentration reduces ramification and surveillance by depolarizing microglia. Exposure to the same K+ concentration (without apyrase added) reduced ramification and surveillance as with apyrase. Dialysis of apyrase to remove K+ retains its ATP-hydrolyzing activity but abolishes the microglial depolarization and decrease of ramification produced by the undialyzed enzyme. Microglia are very sensitive to increases of extracellular ATP concentration, to which they respond by activating P2Y12 receptor-gated THIK-1 K+ channels, generating an outward K+ current which leads to a hyperpolarization of their membrane
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). APY_SOLTU
454
1
50041
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
-
x * 65000-90000, glycosilated protein, x * 48000, deglycosilated protein, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 65000-90000, glycosilated protein, x * 48000, deglycosilated protein, SDS-PAGE
additional information
structure comparison and molecular modelling, evolutionary structural relationships, overview
additional information
-
structure comparison and molecular modelling, evolutionary structural relationships, overview
additional information
-
identification of ACR regions in residues 40-454 possibly involved in metal binding, sequence comparison, and structure analysis and modeling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
hyperglycosylation, mass of glycosylated protein is 65000-90000, mass of deglycosylated protein is 48000 Da
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
development of a two-dimensional array ATP/ADP sensitive image sensor with a uniform distribution of chemically immobilized apyrase, immobilization via the two different methods 3-APTES and CEST, analysis method evaluation and optimization, overview. The surface of the ATP image sensor with 3-APTES method is polluted with the precipitation and shows heterogeneity. The ATP image sensor with CEST method shows a clear surface as well as that before the immobilization of apyrase. Potential disributions, and durability analysis
additional information
-
mutational analysis of residues involved in catalysis, overview
additional information
-
silencing of the apyrase with RNAi constructs under the control of the constitutive 35S promoter leads to a strong decrease in apyrase activity to below 10% of the wild-type level. This decreased activity leads to phenotypic changes in the transgenic lines, including a general retardation in growth, an increase in tuber number per plant, and differences in tuber morphology. Silencing of apyrase under the control of a tuber-specific promoter B33 leads to similar changes in tuber morphology, but not to direct effects of apyrase inhibition on tuber metabolism, phenotypes, overview
additional information
-
immobilization of the enzyme in a two-step process: in the first step, carboxyl group on polyethylene terephthalate (PET) surface is activated by the crosslinker 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride, and in the second step, the enzyme is covalently attached to the activated carboxyl group, method development and evaluation. Kinetic study of NTPDase immobilization and its effect of hemocompatibility on PET, overview. Surface morphology and chemical composition of the unmodified and modified PET films are examined using scanning electron microscope with energy dispersive X-ray spectroscopy analysis
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1% DMSO and 0.01% Tween 20 have no effect on enzyme stability and activity
-
the removal of thioredoxin-tag from purified apyrase causes 10times reduction of specific activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoforms APY4, APY5 and APY6 are expressed in Escherichia coli BL21(DE3) cells with thioredoxin-tag, His6-tag and S-tag
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
isoform APY6 in 50 mM Tris-HCl pH 6.5 buffer containing 6 M guanidine hydrochloride and 10 mM 2-mercaptoethanol
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
usage of the enzyme in a two-dimensional array ATP/ADP sensitive image sensor, with a uniform distribution of chemically immobilized apyrase (via two different methods (3-APTES and CEST)). The enzyme sensor changes ATP into AMP, and the concentration of ATP reduces with time. The time-dependent profile of the potential response is different from the common ion sensor on which the concentration of the analyte ion is constant at an equilibrium state. Two ways of the measurement are used: 1. the addition measurement and 2. the steady measurement, overview
medicine
significant IgG antibody reactivity was observed in sera from patients with American cutaneous leishmaniasis and schistosomiasis using potato apyrase as antigen, development of drug targets or molecular markers
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mancilla, M.; Valenzuela, M.A.; Anich, M.; Kettlun, A.M.; Jara, O.; Traverso-Cori, A.
Identification of an apyrase activating protein and of calmodulin in Solanum tuberosum
Phytochemistry
26
2471-2474
1987
Solanum tuberosum
-
Mancilla, M.; Kettlun, A.M.; Valenzuela, M.A.; Traverso-Cori, A.
Structural studies of two apyrases from Solanum tuberosum
Phytochemistry
23
1397-1400
1984
Solanum tuberosum
-
Haromy, T.P.; Knight, W.B.; Dunaway-Mariano, D.; Sundaralingam, M.
Investigation of structure, protonation, and reactivity of tetraamine(imidodiphosphato)cobalt(III), a substrate for potato apyrase
Biochemistry
22
5015-5021
1985
Solanum tuberosum
-
Kettlun, A.M.; Uribe, L.; Calvo, V.; Silva, S.; Rivera, J.; Mancilla, M.; Valenzuela, M.A.; Traverso-Cori, A.
Properties of two apyrases from Solanum tuberosum
Phytochemistry
21
551-558
1982
Solanum tuberosum
-
Traverso-Cori, A.; Traverso, S.; Reyes, H.
Different molecular forms of potato apyrase
Arch. Biochem. Biophys.
137
133-142
1970
Solanum tuberosum
Komoszynski, M.A.
Comparative studies of animal and plant apyrases (ATP diphosphohydrolase EC 3.6.1.5) with application of immunological techniques and various ATPase inhibitors
Comp. Biochem. Physiol. B
113
581-591
1996
Bos taurus, Hordeum vulgare, Lupinus luteus, Pisum sativum, Secale cereale, Solanum tuberosum, Triticosecale Wittmack, Triticum aestivum, Zea mays
Nourizad, N.; Ehn, M.; Gharizadeh, B.; Hober, S.; Nyren, P.
Methylotrophic yeast Pichia pastoris as a host for production of ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)
Protein Expr. Purif.
27
229-237
2003
Solanum tuberosum
Kettlun, A.M.; Espinosa, V.; Garcia, L.; Valenzuela, M.A.
Potato tuber isoapyrases: substrate specificity, affinity labeling, and proteolytic susceptibility
Phytochemistry
66
975-982
2005
Solanum tuberosum
Kozakiewicz, A.; Neumann, P.; Banach, M.; Komoszy?ski, M.; Wojtczak, A.
Modeling studies of potato nucleoside triphosphate diphosphohydrolase NTPDase1: an insight into the catalytic mechanism
Acta Biochim. Pol.
55
141-150
2008
Solanum tuberosum
Faria-Pinto, P.; Rezende-Soares, F.A.; Molica, A.M.; Montesano, M.A.; Marques, M.J.; Rocha, M.O.; Gomes, J.A.; Enk, M.J.; Correa-Oliveira, R.; Coelho, P.M.; Neto, S.M.; Franco, O.L.; Vasconcelos, E.G.
Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
Parasitology
135
943-953
2008
Schistosoma mansoni (A1BXT9), Schistosoma mansoni, Solanum tuberosum (P80595), Solanum tuberosum
Riewe, D.; Grosman, L.; Fernie, A.R.; Wucke, C.; Geigenberger, P.
The potato-specific apyrase is apoplastically localized and has influence on gene expression, growth, and development
Plant Physiol.
147
1092-1109
2008
Solanum tuberosum
Wujak, M.; Banach, M.; Porowinska, D.; Piskulak, K.; Komoszynski, M.
Isolation and bioinformatic analysis of seven genes encoding potato apyrase. Bacterial overexpresssion, refolding and initial kinetic studies on some recombinant potato apyrases
Phytochemistry
93
8-17
2013
Solanum tuberosum
Endo, S.; Kato, R.; Sawada, K.; Hattori, T.
Two-dimensional array ATP/ADP sensitive image sensor with a uniform distribution of chemically immobilized apyrase
Bull. Chem. Soc. JPN
91
304-310
2018
Solanum tuberosum (P80595)
-
Ramachandran, B.; Muthuvijayan, V.
Kinetic study of NTPDase immobilization and its effect of haemocompatibility on polyethylene terephthalate
J. Biomat. Sci.
30
437-449
2019
Solanum tuberosum
Madry, C.; Arancibia-Carcamo, I.L.; Kyrargyri, V.; Chan, V.T.T.; Hamilton, N.B.; Attwell, D.
Effects of the ecto-ATPase apyrase on microglial ramification and surveillance reflect cell depolarization, not ATP depletion
Proc. Natl. Acad. Sci. USA
115
E1608-E1617
2018
Solanum tuberosum
EXTERNAL LINKS (specific for EC-Number 3.6.1.5)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
