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Information on EC 3.6.1.5 - apyrase and Organism(s) Homo sapiens and UniProt Accession Q5MY95

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.5 apyrase
IUBMB 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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This record set is specific for:
Homo sapiens
UNIPROT: Q5MY95
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ecto-NTPDase
-
ecto-nucleoside triphosphate diphosphohydrolase8
-
ectonucleotidase
-
nucleoside triphosphate diphosphohydrolase
-
nucleoside triphosphate diphosphohydrolase-8
-
5' ectonucleotidase
-
adenosine diphosphatase
-
-
-
-
ADPase
-
-
-
-
APT102
-
-
APY-1
-
-
Apyrase
-
-
ATP-diphosphatase
-
-
-
-
ATP-diphosphohydrolase
-
-
-
-
ATPDase
-
-
-
-
CD39 antigen
-
-
-
-
ecto-nucleoside triphosphate diphosphohydrolase1
-
ecto-nucleoside triphosphate diphosphohydrolase2
-
ecto-nucleoside triphosphate diphosphohydrolase3
-
ectonucleotidase
-
ENTPDase1
-
Golgi nucleoside diphosphatase
-
-
-
-
HB6
-
-
-
-
Lymphoid cell activation antigen
-
-
-
-
NTPDase 2
-
NTPDase1
NTPDase3
nucleoside triphosphate diphosphohydrolase
soluble apyrase
-
-
soluble calcium-activated nucleotidase 1
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
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 hide
9000-95-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a ribonucleoside 5'-triphosphate + H2O
a ribonucleoside 5'-phosphate + 2 phosphate + 2 H+
show the reaction diagram
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
?
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate + H2O
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-phosphate + diphosphate
show the reaction diagram
i.e. PSB-170621A, developement of a selective and highly sensitive capillary electrophoresis (CE) assay using a fluorescent CD39 substrate, a fluorescein-labelled ATP, i.e. N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate that is converted to its AMP derivative (N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-phosphate). To accelerate the assays, a two-directional (forward and reverse) CE system is implemented using 96-well plates, which is suitable for the screening of compound libraries. Achievement of a large enhancement in sensitivity as compared to previous methods (e.g. malachite-green assay: 1000000fold, CE-UV assay: 500000fold, fluorescence polarization immunoassay: 12500fold). The assay is validated by performing inhibition assays with several standard CD39 inhibitors. N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate is preferably hydrolyzed by CD39 as compared to other ectonucleotidases
-
-
ir
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
CDP + H2O
CMP + phosphate
show the reaction diagram
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
GDP + H2O
GMP + phosphate
show the reaction diagram
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate + H2O
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-phosphate + diphosphate
show the reaction diagram
TDP + H2O
TMP + phosphate
show the reaction diagram
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
UDP + 2 H2O
uridine + 2 phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
UTP + 2 H2O
UMP + 2 phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a ribonucleoside 5'-triphosphate + H2O
a ribonucleoside 5'-phosphate + 2 phosphate + 2 H+
show the reaction diagram
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
preferred to Co2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PSB-POM141
i.e. [TiW11CoO40]8-
-
1-amino-4-[(naphthalen-1-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
PSB-06126, an anthraquinone derivative, competitive mechanism of inhibition
ARL 67156
CDTA
-
-
detergent NP-40
at low concentration inhibition of the membrane-bound enzyme, not of the soluble enzyme
dicylcohexylcarbodiimid
-
DCCD, slightly inhibited
EGTA
-
-
fluoride
-
-
NaN3
-
60% inhibition
orthovanadate
p-chloromercuriphenylsulfonic acid
-
1 mM, 56% of inhibition
p-hydroxymercuribenzoate
-
1 mM, 35% of inhibition
PSB-POM141
i.e. [TiW11CoO40]8-
-
Sodium azide
-
hydrolysis of both ATP and ADP
Sodium fluoride
-
20 mM, 50% residual ATPase activity, 56% residual ADPase activity
suramin
-
0.3 mM, 44% residual ATPase activity, 63% residual ADPase activity
Trifluoperazine
-
0.2 mM, 31% residual ATPase activity, 61% residual ADPase activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.081 - 0.226
ATP
pH 7.5, 37°C, recombinant enzyme
0.105
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase8
0.107
ADP
-
pH 8.0, 37°C
0.017 - 0.0776
ATP
0.0133 - 0.0555
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0387
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase8
0.0225 - 0.119
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase8
0.89 - 6.07
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00439
1-amino-4-[(naphthalen-1-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
pH 7.5, 37°C, recombinant enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00776
1-amino-4-[(naphthalen-1-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.17
recombinant chimeric mutant hu-ck ACR1,5
1020
purified recombinant extracellular domain, pH 7.5, in presence of Ca2+
2.33
purified recombinant wild-type enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62
above, enzyme, recombinant soluble His-tagged secreted NTPDase2 extracellular domain
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 60
native full-length enzyme
30 - 62
and above, recombinant soluble His-tagged secreted NTPDase2 extracellular domain
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
HaCaT keratinocyte
Manually annotated by BRENDA team
-
mRNA found in this tissue
Manually annotated by BRENDA team
highest expression
Manually annotated by BRENDA team
-
mRNA found in this tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme contains two transmembrane domains and five apyrase conserved regions, ACRs. ACR1 is located near the N-terminal transmembrane domain, whereas ACR5 is located near the C-terminal transmembrane domain
Manually annotated by BRENDA team
associated with membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENTP8_HUMAN
495
2
53904
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60500
-
radiation-inactivation, ADPase
62000
x * 62000, recombinant soluble His-tagged secreted NTPDase2 extracellular domain, SDS-PAGE
62700
-
radiation-inactivation, ATPase
64000
-
SDS-PAGE
71000
-
-
78000
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 53773, calculated from amino acid sequence
?
x * 62000, recombinant soluble His-tagged secreted NTPDase2 extracellular domain, SDS-PAGE
dimer
-
crosslinking experiments
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C10S
-
112% of wild-type ATPase activity, 105% of wild-type ADPase activity, residue responsible for dimer formation
C10S/C501S
-
148% of wild-type ATPase activity, 133% of wild-type ADPase activity
C10S/C501S/C509S
-
79% of wild-type ATPase activity, 77% of wild-type ADPase activity
C10S/C509S
-
103% of wild-type ATPase activity, 99% of wild-type ADPase activity
C501S
-
130% of wild-type ATPase activity, 130% of wild-type ADPase activity, site of modification by p-chloromercuriphenylsulfonic acid
C501S/C509S
-
138% of wild-type ATPase activity, 134% of wild-type ADPase activity
C509S
-
148% of wild-type ATPase activity, 155% of wild-type ADPase activity
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated by Tween 20
-
unstable to detergent Triton X-100
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, octylglucoside, stable
-
4°C, purified recombinant extracellular domain, stable for several weeks
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially
-
recombinant His-tagged soluble NTPDase2 extracellular domain from HEK-293 cells by ammonium sulfate fractionation, ultrafiltration, nickel affinity chromatography, and gel filtration
reconstitution of enzyme in lipid vesicles is associated with a decrease in KM value of nearly an order of magnitude over the detergent-solubilized form, with a concomitant increase in both ADPase and ATPase catalytic efficiencies
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293T cells and COS-7 cells
recombinant expression of the isozyme in COS-7 cells
CD39, expression in COS-7 cells
-
expression of mutant hu-ck ACR1,5 chimeric enzymes in HEK-293 cells, stable expression of soluble His-tagged secreted NTPDase2 extracellular domain in HEK-293 cells
gene LALP70 cloned into the mammalian expression vector pCl-Neo, expression on the surface of COS-7 cells
-
recombinant expression of human enzyme in C57BL/6 mice
recombinant expression of the isozyme in COS-7 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the NTPDase isozymes are targets for development of potent and selective drug-like NTPDase inhibitors
drug development
the NTPDase isozymes are targets for development of potent and selective drug-like NTPDase inhibitors
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Knowles, A.F.; Isler, R.E.; Reece, J.F.
The common occurrence of ATP diphosphohydrolase in mammalian plasma membranes
Biochim. Biophys. Acta
731
88-96
1983
Canis lupus, Homo sapiens, Mus sp.
Manually annotated by BRENDA team
Biederbick, A.; Kosan, C.; Kunz, J.; Elsaesser, H.P.
First apyrase splice variants have different enzymatic properties
J. Biol. Chem.
275
19018-19024
2000
Homo sapiens
Manually annotated by BRENDA team
Kaczmarek, E.; Koziak, K.; Sevigny, J.; Siegel, J.B.; Anrather, J.; Beaudoin, A.R.; Bach, F.H.; Robson, S.C.
Identification and characterization of CD39/vascular ATP diphosphohydrolase
J. Biol. Chem.
271
33116-33122
1996
Bos taurus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kettlun, A.M.; Alvarez, A.; Quintar, R.; Valenzuela, M.A.; Collados, L.; Aranda, E.; Banda, A.; Chayet, L.; Chiong, M.; Mancilla, M.; Traverso-Cori, A.
Human placental ATP-diphosphohydrolase: biochemical characterization, regulation and function
Int. J. Biochem.
26
437-448
1994
Homo sapiens
Manually annotated by BRENDA team
Shi, J.D.; Kukar, T.; Wang, C.Y.; Li, Q.Z.; Cruz, P.E.; Davoodi-Semiromi, A.; Yang, P.; Gu, Y.; Lian, W.; Wu, D.H.; She, J.X.
Molecular cloning and characterization of a novel mammalian endo-apyrase (LALP1)
J. Biol. Chem.
276
17474-17478
2001
Mus musculus (Q3TCT4), Mus musculus, Homo sapiens (Q9NQZ7), Homo sapiens
Manually annotated by BRENDA team
Murphy, D.M.; Ivanenkov, V.V.; Kirley, T.L.
Identification of cysteine residues responsible for oxidative cross-linking and chemical inhibition of human nucleoside-triphosphate diphosphohydrolase 3
J. Biol. Chem.
277
6162-6169
2002
Homo sapiens
Manually annotated by BRENDA team
Leal, D.B.; Streher, C.A.; Neu, T.N.; Bittencourt, F.P.; Leal, C.A.; da Silva, J.E.; Morsch, V.M.; Schetinger, M.R.
Characterization of NTPDase (NTPDase1; ecto-apyrase; ecto-diphosphohydrolase; CD39; EC 3.6.1.5) activity in human lymphocytes
Biochim. Biophys. Acta
1721
9-15
2005
Homo sapiens
Manually annotated by BRENDA team
Haller, C.A.; Cui, W.; Wen, J.; Robson, S.C.; Chaikof, E.L.
Reconstitution of CD39 in liposomes amplifies nucleoside triphosphate diphosphohydrolase activity and restores thromboregulatory properties
J. Vasc. Surg.
43
816-823
2006
Homo sapiens
Manually annotated by BRENDA team
Chiang, W.C.; Knowles, A.F.
Transmembrane domain interactions affect the stability of the extracellular domain of the human NTPDase 2
Arch. Biochem. Biophys.
472
89-99
2008
Gallus gallus (O93295), Gallus gallus, Homo sapiens (Q9Y5L3), Homo sapiens
Manually annotated by BRENDA team
Uccelletti, D.; Pascoli, A.; Farina, F.; Alberti, A.; Mancini, P.; Hirschberg, C.B.; Palleschi, A.C.
APY-1, a novel Caenorhabditis elegans apyrase involved in unfolded protein response signalling and stress responses
Mol. Biol. Cell
19
1337-1345
2008
Homo sapiens
Manually annotated by BRENDA team
Syed, S.K.; Kauffman, A.L.; Beavers, L.S.; Alston, J.T.; Farb, T.B.; Ficorilli, J.; Marcelo, M.C.; Brenner, M.B.; Bokvist, K.; Barrett, D.G.; Efanov, A.M.
Ectonucleotidase NTPDase3 is abundant in pancreatic beta-cells and regulates glucose-induced insulin secretion
Am. J. Physiol. Endocrinol. Metab.
305
E1319-E1326
2013
Homo sapiens (O75355), Homo sapiens, Mus musculus (Q8BFW6), Mus musculus
Manually annotated by BRENDA team
Rooklin, D.W.; Lu, M.; Zhang, Y.
Revelation of a catalytic calcium-binding site elucidates unusual metal dependence of a human apyrase
J. Am. Chem. Soc.
134
15595-15603
2012
Homo sapiens (Q8WVQ1), Homo sapiens
Manually annotated by BRENDA team
Ho, C.L.; Yang, C.Y.; Lin, W.J.; Lin, C.H.
Ecto-nucleoside triphosphate diphosphohydrolase 2 modulates local ATP-induced calcium signaling in human HaCaT keratinocytes
PLoS ONE
8
e57666
2013
Homo sapiens (Q9Y5L3), Homo sapiens
Manually annotated by BRENDA team
Pelletier, J.; Salem, M.; Lecka, J.; Fausther, M.; Bigonnesse, F.; Sevigny, J.
Generation and characterization of specific antibodies to the murine and human ectonucleotidase NTPDase8
Front. Pharmacol.
8
115
2017
Homo sapiens (Q5MY95), Homo sapiens, Mus musculus (Q8K0L2), Mus musculus
Manually annotated by BRENDA team
Fiene, A.; Baqi, Y.; Lecka, J.; Sevigny, J.; Mueller, C.
Fluorescence polarization immunoassays for monitoring nucleoside triphosphate diphosphohydrolase (NTPDase) activity
Analyst
140
140-148
2015
Homo sapiens (O75355), Homo sapiens (P49961), Homo sapiens (Q5MY95), Homo sapiens (Q9Y5L3)
Manually annotated by BRENDA team
Lee, S.Y.; Luo, X.; Namasivayam, V.; Geiss, J.; Mirza, S.; Pelletier, J.; Stephan, H.; Sevigny, J.; Mueller, C.E.
Development of a selective and highly sensitive fluorescence assay for nucleoside triphosphate diphosphohydrolase1 (NTPDase1, CD39)
Analyst
143
5417-5430
2018
Homo sapiens (O75355), Homo sapiens (P49961), Homo sapiens (Q5MY95), Homo sapiens (Q9Y5L3), Homo sapiens
Manually annotated by BRENDA team
Ji, Y.; Adeola, O.; Strawn, T.L.; Jeong, S.S.; Chen, R.; Fay, W.P.
Recombinant soluble apyrase APT102 inhibits thrombosis and intimal hyperplasia in vein grafts without adversely affecting hemostasis or re-endothelialization
J. Thromb. Haemost.
15
814-825
2017
Homo sapiens
Manually annotated by BRENDA team
Roberts, V.; Campbell, D.J.; Lu, B.; Chia, J.; Cowan, P.J.; Dwyer, K.M.
The differential effect of apyrase treatment and hCD39 overexpression on chronic renal fibrosis after ischemia-reperfusion injury
Transplantation
101
e194-e204
2017
Homo sapiens (P49961), Homo sapiens
Manually annotated by BRENDA team