| Apyrase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| structure and protein design of human apyrase | |||||||||
| Identifiers | |||||||||
| Symbol | Apyrase | ||||||||
| Pfam | PF06079 | ||||||||
| InterPro | IPR009283 | ||||||||
| SCOP | 1s1d | ||||||||
|
|||||||||
Apyrase (adenosine diphosphatase) 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.
The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes are implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate.[1]
This article incorporates text from the public domain Pfam and InterPro IPR009283
|
|||||||||||||||||||||||||||||||||||||||||||||||