nucleoside triphosphate

In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.

In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.

Inosine Triphosphate Pyrophosphatase (ITPase) is a cytoplasmic enzyme that belongs to the HAM1 NTPase family. ITPase hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP) and deoxyinosine triphosphate (dITP) to the monophosphate nucleotide (IMP) and diphosphate. The ITPase enzyme acts as a homodimer and does not distinguish between the deoxy- and ribose forms. ITPase probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. Defects in ITPase is thought to be inherited and is characterized by an over-accumulation of ITP in erythocytes, leukocytes and fibroblasts.

CD39L1 protein (ENTPD2 or NTPDase2) is a member of the ecto-nucleoside triphosphate diphosphohydrolase family which the main role is termination of purinergic signaling. CD39L1 gene encodes a precursor protein with 495 amino acid residues which generates a 437 amino acid residues mature protein after processing. It is an ecto-nucleotidase that found on the surface of vascular adventitial cells and accessory vascular cells. CD39L1 is a Ca2+- and Mg2+-dependent enzyme that activates platelets by preferentially converting ATP to ADP. CD39L1 plays a role in regulating thrombosis and inflammation which is considered to be a therapeutic target for thromboregulation and the treatment of vascular inflammation. Alternative splicing of CD39L1 gene results in multiple transcript variants.

NTPDase 2, also known as ENTPD2, belongs to the ecto-nucleoside triphosphate diphosphohydrolase family (E-NTPDase). Members of E-NTPDase family are nucleotidases able to hydrolyze 5′-nucleoside tri- and or diphosphates; the main role of these enzymes is the termination of purinergic signaling. NTPDases are ubiquitous and were previously shown in other parasites including the trypanosomatides of genus Leishmania and in T. brucei. NTPase activity would act as a timer and is crucial to T. gondii infection. In L. pneumophila it was demonstrated that an E-NTPDase, similar to CD39, is essential for intracellular bacterial multiplication. NTPDase 2 is an integral membrane protein. In the nervous system, it could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Alternative splicing of NTPDase 2 gene results in multiple transcript variants.