Apyrase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Apyrase | ||||||||
Pfam | PF06079 | ||||||||
InterPro | IPR009283 | ||||||||
SCOP2 | 1s1d / SCOPe / SUPFAM | ||||||||
Membranome | 581 | ||||||||
|
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. [1]
Apyrase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Apyrase | ||||||||
Pfam | PF06079 | ||||||||
InterPro | IPR009283 | ||||||||
SCOP2 | 1s1d / SCOPe / SUPFAM | ||||||||
Membranome | 581 | ||||||||
|
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. [1]