EC Number   |
General Information |
Reference |
|---|
    3.6.1.9 | evolution |
ecto-nucleotide pyrophosphatase/phosphodiesterase 1 (NPP1) is a metalloenzyme that belongs to the NPP family, which comprises seven subtypes (NPP1-7) |
757567 |
| 3.6.1.9 | evolution |
ecto-nucleotide pyrophosphatase/phosphodiesterase1 (NPP1) is the most important member of the NPP family, which consists of seven closely related proteins (NPP1-NPP7) |
756172 |
| 3.6.1.9 | evolution |
ecto-nucleotide pyrophosphatase/phosphodiesterase3 (NPP3) belongs to the NPP family, which consists of seven closely related proteins (NPP1-NPP7) |
756172 |
| 3.6.1.9 | evolution |
nucleotide pyrophosphatase/phosphodiesterase (NPP) enzymes belong to the alkaline phosphatase superfamily, with active site characterized by residues of histidine centrally coordinated by divalent cations and serine, cysteine, or threonine residues |
756660 |
| 3.6.1.9 | evolution |
the enzyme belongs to the superfamily of the alkaline phosphatases |
718664 |
| 3.6.1.9 | evolution |
the family II PPase has acquired a pair of nucleotide-binding cystathionine beta-synthase, CBS, domains during evolution, thus endowing the protein with the capacity to be allosterically regulated by adenine nucleotides. Additionally it contains a DRTGG domain between the two CBS domains in the regulatory part, which affords greater flexibility to the regulatory part, allowing it to more rapidly undergo conformational changes in response to binding |
718817 |
| 3.6.1.9 | malfunction |
an npp1 knockout mutant shows shoots and roots larger than those of wild-type seedlings. The starch content in the npp1 mutant shoots is higher than that of wild-type shoots. Growth and starch accumulation are also enhanced under an atmospheric CO2 concentration (40 Pa) when plants were cultured under a 33°C/28°C regime, phenotype, overview. Downregulation of isozyme NPP1 expression is not accompanied by enhancement of AGPase, UGPase and sucrose synthase activities |
730589 |
| 3.6.1.9 | malfunction |
enzyme overexpression results in filamentous cells. The enzyme plays a role in in cell growth inhibition under stress conditions, cell-division arrest and cell-shape maintenance |
735007 |
| 3.6.1.9 | malfunction |
role for NPP1 in insulin receptor signaling: overexpression of NPP1 increases insulin resistance by desensitization of the insulin receptor. Knockdown of NPP1 with siRNA significantly increases insulin-stimulated phosphorylation of tyrosine kinase in a human hepatoma cell line (HUH7) |
756172 |
| 3.6.1.9 | malfunction |
the blockade of NPP1 can increase the concentration of ATP and 2',3''-cGAMP, but at the same time it can decrease the concentration of adenosine by reducing the concentration of its precursor AMP. This all can lead to an enhancement of the immune response in the body. Lentiviral shRNA-knockdown of NPP1 expression in a human glioblastoma cell line (NCH421k cells) reduces cell proliferation, increased accumulation of cells in the G1/G0 cell cycle phase and induced cell death. The mechanism for this effect may be based on the increased activation of cell apoptosis inducing P2X7 receptor activation owing to the accumulation of undegraded ATP (the main substrate of NPP1) by the knockdown of NPP1 function. Furthermore, the reduced production of extracellular adenosine by a blockade of NPP1 function may also reduce the adenosine induced angiogenesis as well as cell proliferation and differentiation by stimulating P1 receptors. Thus, NPP1 inhibitors may have antineoplastic effects on neuronal tumor cells. Increased expression of NPP1 in the chondrocytes, which is age-related, leads to the overproduction of diphosphate |
757567 |
