EC Number   |
General Information |
Reference |
|---|
   1.2.3.1 | metabolism |
3-substituted quinoline triazolopyridine compounds used as c-Met kinase inhibitors are subject to aldehyde oxidase-mediated metabolism. Several compouinds are unstable in monkey liver cytosolic incubations. Small electron-donating groups at the 3-quinoline moiety make the analogs more susceptible to metabolism, whereas large 3-substituents may reverse the trend |
762959 |
| 1.2.3.1 | metabolism |
3-substituted quinoline triazolopyridine compounds used as c-Met kinase inhibitors are subject to aldehyde oxidase-mediated metabolism. Several compounds are unstable in monkey liver cytosolic incubations. Small electron-donating groups at the 3-quinoline moiety make the analogs more susceptible to metabolism, whereas large 3-substituents may reverse the trend |
762959 |
| 1.2.3.1 | metabolism |
aldehyde oxidase catalyzes the final step in the synthesis of abscisic acid and possibly of indole-3-acetic acid |
713323 |
| 1.2.3.1 | metabolism |
density functional theory using the molybdenum cofactor as a model to study structural and energetic aspects of different mechanisms. For a series of 6-substituted 4-quinazolinones, the trend in activation energies is the same for three tested reaction mechanisms. During the transition states for the formation of all possible metabolites for a series of known substrates, the lowest activation energies correspond in all cases to the experimentally observed sites of metabolism |
762552 |
| 1.2.3.1 | metabolism |
IAO1 causes the nonenzymatic conversion of tryptophan to indole-3-acetaldehyde and the enzymatic conversion of indole-3-acetalaldehyde to indole-3-acetic acid |
762824 |
| 1.2.3.1 | metabolism |
nitroaromatic drugs clonazepam, flunitrazepam, flutamide, nilutamide, nimesulide, and nimetazepam are substantially reduced by recombinant AOX1 and human liver cytosol, whereas azelnidipine, nifedipine, and nimodipine are slightly reduced and metronidazole and tolcapone are not reduced. Nitroaromatic drugs reduced by AOX1 possess a relatively electron-deficient nitro group |
762671 |
| 1.2.3.1 | metabolism |
the oxidation of phthalazine reaction involves three sequential steps: protonation of the substrate's N2 atom by Lys893, nucleophilic attack of the hydroxyl group of the molybdenum cofactor (Moco) to the substrate, and hydride transfer from the substrate to the sulfur atom of the Moco. The rate-limiting step corresponds to hydride transfer. Residue Lys893 plays a relevant role in the reaction, being important for the anchorage of the substrate close to the Moco, and also in the catalytic reaction. During the displacement of the products away from the Moco, the transfer of electrons from the catalytic site to the FAD site is proton-coupled. The most favorable and fastest pathway for the enzyme to complete its catalytic cycle is that with MoV and a deprotonated SH ligand of the Moco with the FAD molecule converted to its semiquinone form, FADH radical |
762534 |
| 1.2.3.1 | physiological function |
AOX is up-regulated in the lymphoid organ in response to Vibrio penaeicida at 48 and 72 h after injection |
763460 |
| 1.2.3.1 | physiological function |
AOX2 is the isoform generating the largest rate of superoxide radicals of around 40% in relation to moles of substrate converted |
762958 |
| 1.2.3.1 | physiological function |
AOX3 is an enzyme of well known importance in drug metabolism and therefore of increasing importance in recent drug design programs |
724827 |
