EC Number   |
Substrates |
Organism |
Products |
Reversibility  |
|---|
    3.6.1.5 | more |
Ruviapyrase does not show cytotoxicity against breast cancer (MCF-7) cells and haemolytic activity, it exhibits marginal anticoagulant and strong antiplatelet activity, and dose-dependently reverses the ADP-induced platelet aggregation. The catalytic activity and platelet deaggregation property of Ruviapyrase is significantly inhibited by EDTA, DTT and IAA, and neutralized by commercial monovalent and polyvalent antivenom |
Daboia russelii |
? |
- |
- |
| 3.6.1.5 | more |
adenine nucleotides are the best substrates. The other nucleotides (GTP, UTP, GDP, and UDP) are also hydrolyzed when added to the reaction instead of ATP or ADP, which demonstrates a broad substrate specificity for E-NTPDase expressed on the surface of peritoneal cavity cells |
Mus musculus |
? |
- |
- |
| 3.6.1.5 | more |
APY3-1 exhibits slightly lower enzymatic activity when degrading the ADP compared with ATP, but has very low activity during the degradation of TTP, GTP, and CTP, suggesting that TaAPY3-1 has a high substrate specificity |
Triticum aestivum |
? |
- |
- |
| 3.6.1.5 | more |
development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview |
Homo sapiens |
? |
- |
- |
| 3.6.1.5 | more |
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6 |
Arabidopsis thaliana |
? |
- |
- |
| 3.6.1.5 | more |
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6 |
Arabidopsis thaliana |
? |
- |
- |
| 3.6.1.5 | more |
isozymes NTPDase2 hydrolyzes ATP to ADP, which is released from the enzyme. NTPDase2 shows much higher preference for ATP over ADP, and therefore produces ADP as its main product. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview |
Homo sapiens |
? |
- |
- |
| 3.6.1.5 | more |
isozymes NTPDase3 and -8 hydrolyze ATP to ADP, which is released from the enzyme, and ADP is subsequently hydrolyzed to AMP. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview |
Homo sapiens |
? |
- |
- |
| 3.6.1.5 | more |
isozymes NTPDase3 and -8 hydrolyze ATP to ADP, which is released from the enzyme, and ADP is subsequently hydrolyzed to AMP. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrate, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview |
Homo sapiens |
? |
- |
- |
| 3.6.1.5 | more |
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose) |
Arabidopsis thaliana |
? |
- |
- |
