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Literature summary for 3.6.1.5 extracted from
- The stability of chicken nucleoside triphosphate diphosphohydrolase 8 requires both of its transmembrane domains (2010), Biochemistry, 49, 134-146.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cloning of His-tagged wild-type and mutant NTPDase8s in Escherichia coli strain DH5alpha and stable expression in HEK293 cell plasma membranes | Gallus gallus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | generation of a soluble truncated mutant NTPDase8 by removal of amino acids 1-28 (containing TMD1) and 464-493 (containing TMD2), the mutant shows 85% reduced activity compared to the full-length membrane-bound enzyme. Generation of chimeric mutant Ck-hu TMD1, encoding a protein in which the N-terminus (aa 1-28) of the chicken NTPDase8 is substituted with the corresponding region (aa 1-29) of the human NTPDase2, which includes its TMD1, and of chimeric mutant Ck-hu TMD2, encoding a protein in which the C-terminus (aa 465-493) of the chicken NTPDase8 is substituted with the corresponding region (aa 461-495) of the human NTPDase2, which includes its TMD2 | Gallus gallus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | chicken NTPDase8 is not susceptible to substrate inactivation or agents that cause membrane perturbation, but its soluble mutant, lacking C- and N-termini, is susceptible to inhibition. This inhibition of the mutant can be abolished by mutant enzyme-crosslinking on membranes with glutaraldehyde, the ATPase activities of glutaraldehyde-treated chicken NTPDase8 ECD preincubated with ATP, ADP, and phosphate are respectively 95%, 80%, and 89% of the control | Gallus gallus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cell surface | NTPDase8 is a cell surface ectonucleotidase with a large extracellular domain containing the active site and is anchored to the membrane by two transmembrane domains at the N- and C-termini | Gallus gallus | 9986 | - |
| membrane | NTPDase8 is a cell surface ectonucleotidase with a large extracellular domain containing the active site and is anchored to the membrane by two transmembrane domains at the N- and C-termini | Gallus gallus | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Gallus gallus |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + H2O | Gallus gallus | - |
AMP + phosphate | - |
? | |
| ATP + 2 H2O | Gallus gallus | - |
AMP + 2 phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gallus gallus | O93295 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant NTPDase8s from HEK293 cell plasma membranes by ammonium sulfate fractionation and nickel affinity column chromatography | Gallus gallus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + H2O | - |
Gallus gallus | AMP + phosphate | - |
? | |
| ATP + 2 H2O | - |
Gallus gallus | AMP + 2 phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | NTPDase8 is a cell surface ectonucleotidase with a large extracellular domain containing the active site and is anchored to the membrane by two transmembrane domains at the N- and C-termini | Gallus gallus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATPase | - |
Gallus gallus |
| NTPDase8 | - |
Gallus gallus |
| nucleoside triphosphate diphosphohydrolase 8 | - |
Gallus gallus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Gallus gallus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 15 | 60 | activity range, the activity of the full-length enzyme increases with temperature up to 60°C, whereas the ATPase activity of the mutant truncated NTPDase8 ECD decreases at temperatures higher than 25°C even when assayed for 1 min | Gallus gallus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
the pH optimum of MgATPase of the wild-type full-length chicken NTPDase8 is in the neutral pH range while the pH optimum of the mutant MgADPase activity is more acidic at about pH 6.0 | Gallus gallus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
the MgATPase/MgADPase ratio of the full-length chicken NTPDase8 varies widely with pH, overview | Gallus gallus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | a soluble truncated mutant NTPDase8, lacking the extracellular domain, shows 85% reduced activity compared to the full-length membrane-bound enzyme. Also activity of the soluble chicken NTPDase8 decreases with time in a temperature-dependent manner as a result of inactivation by ATP, ADP, and phosphate, in contrast to the wild-type full-length enzyme | Gallus gallus |
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