page_title: Apyrase
hierarchical_section_title: Apyrase
caption_attribution_description: English: Cartoon representation of the molecular structure of protein registered with 1s18 code. Deutsch: Grafik des Molekularstruktur von jenem Protein, das mit 1s18 code registriert ist. Plattdüütsch: Grafik, de de Molekularstruktur von dat Protein wiest, dat mit’n Kood 1s18 registreert is.
context_page_description: Apyrase is a calcium-activated plasma membrane-bound enzyme that catalyses the hydrolysis of ATP to yield AMP and inorganic phosphate. Two isoenzymes are found in commercial preparations from S. tuberosum. One with a higher ratio of substrate selectivity for ATP:ADP and another with no selectivity.
  It can also act on ADP and other nucleoside triphosphates and diphosphates with the general reaction being NTP -> NDP + Pi -> NMP + 2Pi. This is the same activity that has been employed in the degradation of unincorporated nucleosides during pyrosequencing.
  The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes that are implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate.
context_section_description: Apyrase (EC 3.6.1.5, ATP-diphosphatase, adenosine diphosphatase, ADPase, ATP diphosphohydrolase) is a calcium-activated plasma membrane-bound enzyme (magnesium can also activate it) (EC 3.6.1.5) that catalyses the hydrolysis of ATP to yield AMP and inorganic phosphate. Two isoenzymes are found in commercial preparations from S. tuberosum. One with a higher ratio of substrate selectivity for ATP:ADP (approx 10) and another with no selectivity (ratio 1).
  It can also act on ADP and other nucleoside triphosphates and diphosphates with the general reaction being NTP -> NDP + Pi -> NMP + 2Pi. This is the same activity that has been employed in the degradation of unincorporated nucleosides during pyrosequencing.
  The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes that are implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate.
caption: structure and protein design of human apyrase
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