NTPDase

Ectonucleotidases (also known as NTPDases, Ecto-ATPases, ectonucleoside triphosphate diphosphohydrolase) are constitutively expressed ectoenzymes that hydrolyze extracellular nucleotides. There are four known major families of ectonucleotidases.

Products
Background
Literature
Gene Data

Inhibitors

Cat No Product Name / Activity
3633 Adenosine 5'-(α,β-methylene)diphosphate sodium salt
Ecto-5'-nucleotidase (CD73) inhibitor
1283 ARL 67156 trisodium salt
NTPDase inhibitor
2689 POM 1
Inhibitor of E-NTPDases
2574 PSB 06126
NTPDase 3 inhibitor
2573 PSB 069
Non-selective NTPDase inhibitor
6083 PSB 12379
Ecto-5'-nucleotidase (CD73) inhibitor

Ectonucleotidases (also known as NTPDases, Ecto-ATPases, ectonucleoside triphosphate diphosphohydrolase) are ectoenzymes that hydrolyze extracellular nucleotides. There are four major families of ectonucleotidases: CD39/NTPDases (ecto-nucleotide triphosphate diphosphohydrolases); ecto-nucleotide pyrophosphatase phosphodiesterases (E-NPPs); alkaline phosphatases; and ecto-5'-nucleotidases/CD73.

NTPDases are constitutively expressed in many tissues and can be differentiated on the basis of cellular location. NTPDases 1, 2, 3 and 8 are located on the cell surface; NTPDases 5 and 6 are localized within the cell and undergo secretion after heterologous expression; and NTPDases 4 and 7 are entirely intracellularly located and face the lumen of cytoplasmic organelles. NTPDases located at the cell surface require Ca2+ or Mg2+ ions for activity. These subtypes contribute to the recycling of nucleosides from salvage pathways and extracellular nucleoside phosphates.

Due to their role in nucleotide metabolism, NTPDases help control the availability of extracellular nucleotide agonists at P2 receptors and modulate P2 receptor function as a result. The distribution of P2 receptors throughout the body, and the wide-spread nature of purinergic signaling, suggests a vital role for NTPDases in a range of cellular processes. For example, NTPDase1 - the predominant ectonucleotidase in vasculature - has therapeutic potential in alleviating thrombotic and inflammatory stress. NTPDases are also found throughout the nervous system, where they have been shown to directly control the function of the P2 receptors there.

Location, substrate preference and hydrolysis rates vary between subtypes; however, all NTPDases contain five highly conserved sequence domains, known as apyrase conserved regions (APCR1 to APCR5).

Literature for NTPDase

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NTPDase Gene Data

Gene Species Gene Symbol Gene Accession No. Protein Accession No.
NTPDase 1 Human ENTPD1 NM_001776 S73813
Mouse Entpd1 NM_009848 P55772
Rat Entpd1 NM_022587 P97687
NTPDase 2 Human ENTPD2 NM_203468 U91510
Mouse Entpd2 NM_009849 O55026
Rat Entpd2 NM_172030 O35795
NTPDase 3 Human ENTPD3 NM_001248 AF039917
Mouse Entpd3 NM_178676 Q8BFW6
Rat Entpd3 NM_178106 Q80Z26
NTPDase 4 Human ENTPD4 NM_004901 AJ131358
Mouse Entpd4 NM_026174 Q9DBT4
Rat Entpd4 NM_001108384 NP_001101854
NTPDase 5 Human ENTPD5 NM_001249 AF039918
Rat Entpd5 NM_199394 NP_955426
NTPDase 6 Rat Entpd6 NM_053498 NP_445950
NTPDase 7 Human ENTPD7 NM_020354 AF269255
Mouse Entpd7 NM_053103 Q3TCT4
Rat Entpd7 NM_001107595 NP_001101065
NTPDase 8 Human ENTPD8 NM_198585 AY359088
Mouse Entpd8 NM_028093 Q8K0L2
Rat Entpd8 NM_001033565 Q5DRK1