1.2.3.1: aldehyde oxidase
This is an abbreviated version!
For detailed information about aldehyde oxidase, go to the full flat file.
Word Map on EC 1.2.3.1
-
1.2.3.1
-
xanthine
-
molybdenum
-
allopurinol
-
oxidases
-
menadione
-
benzaldehyde
-
abscisic
-
n-oxide
-
n-heterocyclic
-
moco
-
phthalazine
-
raloxifene
-
molybdenum-containing
-
xanthinuria
-
hydralazine
-
oxidase-mediated
-
drug-drug
-
molybdoenzymes
-
sulphite
-
o6-benzylguanine
-
molybdopterin
-
flavin-containing
-
disulfiram
-
n1-methylnicotinamide
-
oxypurinol
-
nutrition
-
medicine
-
hypouricemia
-
amidoxime
-
oxidase-catalyzed
-
pharmacology
-
synthesis
-
degradation
-
cyp2a6
-
nitroreduction
-
imidacloprid
-
neonicotinoids
-
phenanthridine
- 1.2.3.1
- xanthine
- molybdenum
- allopurinol
- oxidases
- menadione
- benzaldehyde
-
abscisic
- n-oxide
-
n-heterocyclic
- moco
- phthalazine
- raloxifene
-
molybdenum-containing
-
xanthinuria
- hydralazine
-
oxidase-mediated
-
drug-drug
-
molybdoenzymes
- sulphite
- o6-benzylguanine
- molybdopterin
-
flavin-containing
- disulfiram
- n1-methylnicotinamide
- oxypurinol
- nutrition
- medicine
-
hypouricemia
-
amidoxime
-
oxidase-catalyzed
- pharmacology
- synthesis
- degradation
- cyp2a6
-
nitroreduction
- imidacloprid
-
neonicotinoids
- phenanthridine
Reaction
Synonyms
Aao4, AHO2, aldehyde oxidase 1, aldehyde oxidase 2, aldehyde oxidase 3, aldehyde oxidase 3-like 1, aldehyde oxidase 4, aldehyde-oxygen oxidoreductase, aldehyde:oxygen oxidoreductase, ALOD, AlOx, antennae-specific aldehyde oxidase, AO, AO-alpha, AO-beta, AO-delta, AO-gamma, AO-kappa, AO1, AO2, AO3, AO4, AOH, AOH1, AOH2, AOH3, AOMM, AOR, AOX, AOX1, AOX2, AOX3, AOX4, AtraAOX2, EC 1.2.3.11, FOD, formate oxidase, IAO1, mAOX3, mouse liver aldehyde oxidase 3, quinoline oxidase, Retinal oxidase, retinene oxidase
ECTree
Advanced search results
General Information
General Information on EC 1.2.3.1 - aldehyde oxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
metabolism
physiological function
aldehyde oxidase catalyzes the final step in the synthesis of abscisic acid and possibly of indole-3-acetic acid
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
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
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
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
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
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
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
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
-
AOX3 is an enzyme of well known importance in drug metabolism and therefore of increasing importance in recent drug design programs
physiological function
AtraAOX2 could be involved in detoxifying plant-derived toxic aldehydes and aldehyde-containing pesticides
physiological function
exogenous application of several aldehydes to siliques in AAO4 knockout plants induces severe tissue damage and enhance malondialdehyde levels and senescence symptoms, but not in wild-type siliques. Abiotic stresses such as dark and ultraviolet C irradiation causes an increase in endogenous reactive carbonyl species and higher expression levels of senescence marker genes, leading to premature senescence of knockout siliques. In naturally senescent knockout siliques, higher endogenous reactive carbonyl species levels are associated with enhanced senescence molecular markers, chlorophyll degradation, and earlier seed shattering compared with the wild type
physiological function
the amount of AOX1 in human liver is similar to rabbit liver, while the metabolism of methotrexate in rabbit liver cytosol is several orders of magnitude higher than any of the other species tested
physiological function
the amount of AOX1 in human liver is similar to rabbit liver, while the metabolism of methotrexate in rabbit liver cytosol is several orders of magnitude higher than any of the other species tested
physiological function
AOX is up-regulated in the lymphoid organ in response to Vibrio penaeicida at 48 and 72 h after injection
physiological function
AOX2 is the isoform generating the largest rate of superoxide radicals of around 40% in relation to moles of substrate converted
physiological function
change in the expression of isoform AO1 is parallel to the abrupt change in indole 3-acetic acid level between 4-7 days after flowering. AO1 is coexpressed with flavin monooxygenases YUCCA9 and YUCCA11
physiological function
-
identification of six putative AOX genes from cotton bollworm, Helicoverpa armigera
physiological function
in vitro reaction of 5-nitroquinoline with AOX under aerobic conditions generates the oxidized 2-oxo-5-nitroquinoline, the reduced 5-aminoquinoline and the oxidized/reduced 2-oxo-5-aminoquinoline metabolites. In human liver cytosol, coincubation of 5-nitroquinoline and AOX oxidative substrates N-(2-(dimethylamino)ethyl)acridine-4-carboxamide and phthalazine significantly increases the yield of the reduced metabolite, while oxidized metabolites production are lowered