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
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1.2.3.1
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xanthine
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molybdenum
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allopurinol
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oxidases
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menadione
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benzaldehyde
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abscisic
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n-oxide
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n-heterocyclic
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moco
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phthalazine
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raloxifene
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molybdenum-containing
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xanthinuria
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hydralazine
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oxidase-mediated
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drug-drug
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molybdoenzymes
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sulphite
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o6-benzylguanine
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molybdopterin
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flavin-containing
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disulfiram
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n1-methylnicotinamide
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oxypurinol
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nutrition
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medicine
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hypouricemia
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amidoxime
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oxidase-catalyzed
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pharmacology
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synthesis
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degradation
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cyp2a6
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nitroreduction
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imidacloprid
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neonicotinoids
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phenanthridine
- 1.2.3.1
- xanthine
- molybdenum
- allopurinol
- oxidases
- menadione
- benzaldehyde
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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
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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
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Application
Application on EC 1.2.3.1 - aldehyde oxidase
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degradation
medicine
nutrition
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identification of 17 diet-derived constituents as inhibitors, with Kiss that vary approximately 300fold. Inhibitors bind within the active site and elucidate key enzyme-inhibitor interactions. QSAR modeling identified three structural descriptors that correlate with inhibition potency
pharmacology
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metabolic inactivation of neonicotinoid insecticide substrates by enzyme system coupled with Drosophila nicotinic acetylcholine receptor
synthesis
additional information
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aldehyde oxidase plays a critical role in nitrite reduction, and this process is regulated by pH, oxygen tension, nitrite, and reducing substrate concentrations
degradation
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the enzyme plays a dual role in the metabolism of physiologically important endogenous compounds and the biotransformation of xenobiotics. Simple qualitative method using density functional theory to predict the product of aldehyde oxidase metabolism by examining the energetics of likely tetrahedral intermediates resulting from nucleophilic attack on carbon
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surgical stress model of oxidative stress in retinoid metabolism, prevention of alterations in enzyme activity and alkaline phosphatase activity by inhibition of superoxide generation using allopurinol
medicine
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adiponectin and fenobibric acid reduce enzyme isoform AOX1 by activating peroxisome proliferator-activated receptor alpha whereas fatty liver disease is associated with elevated hepatic AOX1 level
medicine
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measurements of NMN and its pyridones usually excreted in the urine can be used to predict the in vivo activity of enzyme
medicine
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aldehyde oxidase activity in rats estimated on the basis of benzaldehyde, N1-methylnicotinamide and methotrexate oxidase activities rapidly increases from birth, reaching a plateau within 4 weeks, and is regulated by expression of the protein. Aldehyde oxidase plays an important role in metabolizing many drugs that may be administered to pediatric patients. Developmental changes are important for the clinical application in infants of methotrexate and other drugs that are detoxified by aldehyde oxidase
medicine
aldehyde oxidase can be an important basal source of superoxide that will be enhanced in disease settings where cellular aldehyde levels are increased
medicine
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aldehyde oxidase plays an important role in metabolizing many drugs, so aldehyde oxidase activity in individual patients may be a useful parameter for dose adjustment to avoid severe toxicity. Aldehyde oxidase activity is immature in children below 1 year of age, dose adjustment based on individual aldehyde oxidase activity shall be made for such patients
medicine
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aldehyde oxidases represent an important drug-metabolizing system in the cytosol of the hepatic cell. AOX1 is potentially useful in the bioactivation of pro-drugs in human liver and lung, given that the two tissues are the only ones reported to express significant amounts of this enzymatic activity. Variability in the levels of liver aldehyde oxidase in the human population
medicine
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AOX1 may affect plasma HDL levels by altering ATP-binding cassette transporter A1 activity
medicine
significant correlations between reduced AOX1 expression and tumor stage, or metastatic or regional lymph node states. Reduced expression of AOX1 in malignant transformed hepatocytes supports the differentiation dependent upregulation of AOX1
medicine
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combined computational and experimental investigation of drug-like molecules that are potential aldehyde oxidase substrates and identification of multiple sites of metabolism mediated by AOX
medicine
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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
medicine
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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
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in shake-flask cultures, recombinant Klebsiella pneumoniae expressing the enzyme produces 0.89 g 3-hydroxypropionate per l, i.e. 3 g 3-hydroxypropionate per l during 24 h fed-batch cultivation in a 5 l bioreactor
synthesis
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in shake-flask cultures, recombinant Klebsiella pneumoniae expressing the enzyme produces 0.89 g 3-hydroxypropionate per l, i.e. 3 g 3-hydroxypropionate per l during 24 h fed-batch cultivation in a 5 l bioreactor
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96% amino acid identity with those of human enzyme. Two forms of aldehyde oxidase in monkey are the expression products by a single gene due to possibly existence of two aldehyde oxidase isoforms or two active sites in a single enzyme
additional information
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96% amino acid identity with those of human enzyme. Two forms of aldehyde oxidase in monkey are the expression products by a single gene due to possibly existence of two aldehyde oxidase isoforms or two active sites in a single enzyme
additional information
aldehyde oxidase is involved in the chemo-reception of pheromonal stimuli in the antennae
additional information
despite divergent evolution, AOXs from the molybdo-flavoenzyme family can share a common function in insects and vertebrates, i.e. the control of the duration and/or strength of olfactory stimuli
additional information
despite divergent evolution, AOXs from the molybdo-flavoenzyme family can share a common function in insects and vertebrates, i.e. the control of the duration and/or strength of olfactory stimuli
additional information
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despite divergent evolution, AOXs from the molybdo-flavoenzyme family can share a common function in insects and vertebrates, i.e. the control of the duration and/or strength of olfactory stimuli
additional information
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rat strains with low aldehyde oxidase activity show only a monomer, whereas strains with high activity overwhelmingly exhibit a dimer. Expression levels of aldehyde oxidase homodimer are primarily responsible for rat strain differences in aldehyde oxidase activity
additional information
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variations in the levels of aldehyde oxidase activity in different strains of experimental animals
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals
additional information
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variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens
additional information
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variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens
additional information
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variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens
additional information
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variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
-
despite divergent evolution, AOXs from the molybdo-flavoenzyme family can share a common function in insects and vertebrates, i.e. the control of the duration and/or strength of olfactory stimuli
-