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Information on EC 1.2.3.1 - aldehyde oxidase and Organism(s) Rattus norvegicus and UniProt Accession Q5QE78
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1.2.3.1 aldehyde oxidaseIUBMB Comments
Contains molybdenum, [2Fe-2S] centres and FAD. The enzyme from liver exhibits a broad substrate specificity, and is involved in the metabolism of xenobiotics, including the oxidation of N-heterocycles and aldehydes and the reduction of N-oxides, nitrosamines, hydroxamic acids, azo dyes, nitropolycyclic aromatic hydrocarbons, and sulfoxides [4,6].
The enzyme is also responsible for the oxidation of retinal, an activity that was initially attributed to a distinct enzyme (EC 1.2.3.11, retinal oxidase) [5,7].
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Word Map
- 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
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
aldehyde oxidase, aldehyde oxidase 1, retinal oxidase, formate oxidase, maox3, atraaox2, aldehyde oxidase 3, aldehyde oxidase 2, aldehyde:oxygen oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde oxidase 1
AOX1
quinoline oxidase
-
-
-
-
Retinal oxidase
-
-
-
-
retinene oxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
aldehyde:oxygen oxidoreductase
Contains molybdenum, [2Fe-2S] centres and FAD. The enzyme from liver exhibits a broad substrate specificity, and is involved in the metabolism of xenobiotics, including the oxidation of N-heterocycles and aldehydes and the reduction of N-oxides, nitrosamines, hydroxamic acids, azo dyes, nitropolycyclic aromatic hydrocarbons, and sulfoxides [4,6].
The enzyme is also responsible for the oxidation of retinal, an activity that was initially attributed to a distinct enzyme (EC 1.2.3.11, retinal oxidase) [5,7].
CAS REGISTRY NUMBER
COMMENTARY
9029-07-6
-
9033-52-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-RS-8359 + H2O + O2
2-keto-(S)-RS-8359 + H2O2
Donryu rats show a dimorphic pattern for the 2-oxidation activity of RS-8359
-
-
?
benzaldehyde + H2O + O2
benzoate + H2O2
-
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + H2O2
-
-
-
?
(S)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine + H2O + O2
? + H2O2
-
i.e. S-8359
-
-
?
1-methoxy-2-naphthaldehyde + H2O + O2
1-methoxy-2-naphthoic acid + H2O2
-
-
-
-
?
2-[(6-[[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-a]pyridin-3-yl]sulfanyl]quinolin-3-yl)amino]ethan-1-ol + H2O + O2
? + H2O2
-
-
-
-
?
3 brimonidine + 4 H2O + 4 O2
2-oxobrimonidine + 3-oxobrimonidine + 2,3-dioxobrimonidine + 4 H2O2
-
-
-
-
?
3-methoxy-2-naphthaldehyde + H2O + O2
3-methoxy-2-naphthoic acid + H2O2
-
-
-
-
?
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine + H2O + O2
? + H2O2
-
i.e. RS-8359, 2-oxidation of the S-enantiomer
-
-
?
4-(dimethylamino)cinnamaldehyde + nitrite + H2O + O2
? + nitric oxide
-
in the presence of typical aldehyde substrates like 4-(dimethylamino)cinnamaldehyde or NADH, aldehyde oxidase reduces nitrite to nitric oxide
-
-
?
6-dimethyloamino-2-naphthaldehyde + H2O + O2
6-dimethylamino-2-naphthoic acid + H2O2
-
-
-
-
?
6-methoxy-2-naphthaldehyde + H2O + O2
6-methoxy-2-naphthoic acid + H2O2
-
-
-
-
?
6-[[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-a]pyridin-3-yl]sulfanyl]-N-(oxetan-3-yl)quinolin-3-amine + H2O + O2
? + H2O2
-
-
-
-
?
6-[[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-a]pyridin-3-yl]sulfanyl]-N-(oxolan-3-yl)quinolin-3-amine + H2O + O2
? + H2O2
-
-
-
-
?
6-[[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-a]pyridin-3-yl]sulfanyl]-N-[(oxolan-3-yl)methyl]quinolin-3-amine + H2O + O2
? + H2O2
-
-
-
-
?
6-[[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-a]pyridin-3-yl]sulfanyl]quinoline + H2O + O2
? + H2O2
-
-
-
-
?
7-methoxy-1-naphthaldehyde + H2O + O2
7-methoxy-2-naphthoic acid + H2O2
-
-
-
-
?
acetophenone oxime + H2O + 2-hydroxypyrimidine
acetophenone + NH3
-
-
-
-
?
anthracene-9-carboxaldehyde + H2O + O2
anthracene-9-carboxylate + H2O2
-
-
-
-
?
benzaldehyde + 2 ferricyanide + H2O
benzoate + 2 ferrocyanide + 2 H+
-
-
-
-
?
clothianidin + NMNH
nitroso-clothianidin + amino-clothianidin + ?
-
-
-
-
?
electron donor + nicotinamide N-oxide
nicotinamide + electron acceptor
-
2-hydroxypyrimidine as electron acceptor
-
-
?
imidacloprid + H2O + O2 + N-methylnicotinamide
nitroso-imidacloprid + amino-imidacloprid + H2O2 + ?
imidacloprid + NMNH
nitroso-imidacloprid + amino-imidacloprid + ?
-
-
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + ?
-
variations in the ratio of the amount of pyridones to the total amount of NMN and pyridones in urine are closely related to the enzyme activity
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + H2O2
NADH + nitrite + H2O + O2
? + nitric oxide
-
in the presence of typical aldehyde substrates like 4-(dimethylamino)cinnamaldehyde or NADH, aldehyde oxidase reduces nitrite to nitric oxide. NADH reacts with aldehyde oxidase at the FAD site of the enzyme
-
-
?
phenanthrene-9-carboxaldehyde + H2O + O2
phenanthrene-9-carboxylate + H2O2
-
-
-
-
?
phenanthridine + H2O + O2
?
-
inhibitory effects of 15 flavonoids on the activity of rat liver aldehyde oxidase assessed, glycosylated flavonoids show relatively weaker inhibition, quantitative structureactivity relationship studies performed to elucidate the important structural properties responsible for the observed inhibitory effects
-
-
?
zebularine + H2O + O2
uridine + H2O2
-
-
major catabolic route for oral antitumor agent zebularine
-
?
(S)-RS-8359
?
-
enzyme shows a monophasic pattern in Eadie-Hofstee plots of the (S)-enantiospecific 2-oxidation activity of RS-8359
-
-
?
(S)-RS-8359 + H2O + O2
2-keto-(S)-RS-8359 + H2O2
i.e. 4-([(7S)-7-hydroxy-6,7-dihydro-5H-cyclopenta[d]pyrimidin-4-yl]amino)benzonitrile, reversible inhibitor of monoamine oxidase A. Remarkable strain differences in activity on substrate, correlating in part with expressed levels of protein
-
-
?
(S)-RS-8359 + H2O + O2
2-keto-(S)-RS-8359 + H2O2
Donryu rats show a dimorphic pattern for the 2-oxidation activity of RS-8359
-
-
?
benzaldehyde + H2O + O2
benzoate + H2O2
-
-
-
?
imidacloprid + H2O + O2 + N-methylnicotinamide
nitroso-imidacloprid + amino-imidacloprid + H2O2 + ?
-
-
-
?
imidacloprid + H2O + O2 + N-methylnicotinamide
nitroso-imidacloprid + amino-imidacloprid + H2O2 + ?
-
-
in presence of N-methylnicotinamide, ratio of amino- to nitroso-products is 23 to 14
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + H2O2
-
-
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + H2O2
-
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + H2O2
-
-
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + H2O2
-
-
-
?
additional information
?
-
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
-
enzyme plays an important role in the biotransformation of drugs and xenobiotics, e.g. antiviral, antimalarial and antitumour compounds and nicotine
-
-
?
additional information
?
-
enzyme plays an important role in the biotransformation of drugs and xenobiotics, e.g. antiviral, antimalarial and antitumour compounds and nicotine
-
-
?
additional information
?
-
enzyme is of interest as a source of the reactive oxygen species, hydrogen peroxide and the superoxide anion
-
-
?
additional information
?
-
-
a wide variety of xenobiotics may serve as electron acceptors instead of molecular oxygen. Enzyme reduces nitroguanidines to both nitroso- and aminoguanidines, while nitromethylens are reduced only to the corrsponding nitroso metabolites. Reduction of nitroguanidines to amino metabolites depends on enzyme concentration
-
-
?
additional information
?
-
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
-
phenanthridine N-oxide is not metabolized by the enzyme
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 brimonidine + 4 H2O + 4 O2
2-oxobrimonidine + 3-oxobrimonidine + 2,3-dioxobrimonidine + 4 H2O2
-
-
-
-
?
additional information
?
-
-
enzyme plays an important role in the biotransformation of drugs and xenobiotics, e.g. antiviral, antimalarial and antitumour compounds and nicotine
-
-
?
additional information
?
-
enzyme plays an important role in the biotransformation of drugs and xenobiotics, e.g. antiviral, antimalarial and antitumour compounds and nicotine
-
-
?
additional information
?
-
enzyme is of interest as a source of the reactive oxygen species, hydrogen peroxide and the superoxide anion
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adiponectin
downregulates AOX1 expression by activating peroxisome proliferator-activated receptor-alpha
-
selenium
-
enzyme activity towards substrates (S)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine and vanillin is increased by selenium deficiency to 250% of initial rate, and this corresponds to an increase of Aox1 protein level, but not to a decrease in mRNA level
raloxifene
-
aldehyde oxidase inhibitor, significantly decreases NO generation from nitrite in heart or liver
raloxifene
-
inhibits substrate binding at the molybdenum site of the enzyme
additional information
-
low aldehyde oxidase activity groups are the Slc:Wistar, Crl:SD, F344/DuCrlCrlj, and Slc:SD strains
-
additional information
-
under alkaline conditions, prominent inhibition of NO generation by aldehyde oxidase occurs
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methyl methanesulfonate
causes induction of liver aldehyde oxidase
N-methyl-N'-nitro-N-nitrosoguanidine
causes induction of liver aldehyde oxidase
N-methyl-N-nitrosourea
causes induction of liver aldehyde oxidase
methyl methanesulfonate
causes induction of liver aldehyde oxidase
N-methyl-N'-nitro-N-nitrosoguanidine
causes induction of liver aldehyde oxidase
N-methyl-N-nitrosourea
causes induction of liver aldehyde oxidase
additional information
-
fatty liver disease is associated with elevated hepatic AOX1
-
additional information
fatty liver disease is associated with elevated hepatic AOX1
-
additional information
fatty liver disease is associated with elevated hepatic AOX1
-
additional information
fatty liver disease is associated with elevated hepatic AOX1
-
additional information
fatty liver disease is associated with elevated hepatic AOX1
-
additional information
-
high aldehyde oxidase activity groups are the WKAH/Hkm, WKY/Izm, LEW/CrlCrlj, Crlj:WI, Jcl:Wistar, and Wistar-Imamichi strains
-
additional information
-
under acidic conditions or with mild hypoxia increased NO generation by aldehyde oxidase occurs. NO formation by aldehyde oxidase increases linearly with the increase in nitrite concentration
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0055
2-[(6-[[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-a]pyridin-3-yl]sulfanyl]quinolin-3-yl)amino]ethan-1-ol
-
liver cytosol, pH not specified in the publication, temperature not specified in the publication
-
0.0096
4-(dimethylamino)cinnamaldehyde
-
in the presence of 1 mM nitrite, at pH 6.0 and 37°C
0.001
6-[[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-a]pyridin-3-yl]sulfanyl]-N-(oxetan-3-yl)quinolin-3-amine
-
liver cytosol, pH not specified in the publication, temperature not specified in the publication
-
0.0011
6-[[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-a]pyridin-3-yl]sulfanyl]-N-(oxolan-3-yl)quinolin-3-amine
-
liver cytosol, pH not specified in the publication, temperature not specified in the publication
-
0.004
6-[[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-a]pyridin-3-yl]sulfanyl]-N-[(oxolan-3-yl)methyl]quinolin-3-amine
-
liver cytosol, pH not specified in the publication, temperature not specified in the publication
-
0.064
6-[[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-a]pyridin-3-yl]sulfanyl]quinoline
-
liver cytosol, pH not specified in the publication, temperature not specified in the publication
-
0.0341
(S)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
pH 7.4, 37°C
0.0407
(S)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
pH 7.4, 37°C, enzyme isolated from animals fed with a selenium-deficient diet
0.0804
(S)-RS-8359
pH 7.4, 37°C, enzyme from Wistar-Imamichi strain, ratio Vmax/Km 1.98 microl per min and mg
0.0813
(S)-RS-8359
pH 7.4, 37°C, enzyme from Jcl:Wistar strain, ratio Vmax/Km 1.00 microl per min and mg
0.0833
(S)-RS-8359
pH 7.4, 37°C, enzyme from Crj:Wistar strain, ratio Vmax/Km 1.46 microl per min and mg
0.1046
(S)-RS-8359
pH 7.4, 37°C, enzyme from LEW:Crj strain, ratio Vmax/Km 0.58 microl per min and mg
0.14
(S)-RS-8359
pH 7.4, 37°C, enzyme from F344/DuCrj strain, ratio Vmax/Km 0.01 microl per min and mg
0.17
(S)-RS-8359
pH 7.4, 37°C, enzyme from Slc:SD strain, ratio Vmax/Km 0.09 microl per min and mg
0.173
(S)-RS-8359
pH 7.4, 37°C, enzyme from Crj:SD strain, ratio Vmax/Km 0.06 microl per min and mg
0.0043
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
chimeric rat/monkey enzyme, high affinity value, pH 6.0, 37°C
0.0171
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
chimeric rat/monkey enzyme, low affinity value, pH 6.0, 37°C
0.0363
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
chimeric monkey/rat enzyme, pH 6.0, 37°C
0.0528
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
wild-type, pH 6.0, 37°C
0.355
N-methylnicotinamide
female rat liver enzyme after reduction with DTT
0.36
N-methylnicotinamide
male rat liver enzyme after reduction with DTT
1.895
N-methylnicotinamide
female rat liver enzyme after reduction with DTT and reoxidation with 4,4'-dithiodipyridine
3.3
nitrite
-
in the presence of 0.05 mM 4-(dimethylamino)cinnamaldehyde, at pH 6.0 and 37°C
0.0158
Vanillin
-
pH 7.4, 37°C, enzyme isolated from animals fed with a selenium-deficient diet
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
maximum aldehyde oxidase-catalyzed nitric oxide generation occurs at pH 6.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
maximum aldehyde oxidase-catalyzed nitric oxide generation occurs at pH 6.0. When the pH is decreased to 5.0 or increased above 8.0, a decrease in the rate of nitric oxide generation is observed
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
distribution of the activity is uneven, being seen mainly in the pericentral rather than the periportal area
-
-
390370, 390374, 390380, 390388, 390399, 390415, 672548, 673058, 691162, 693075, 695270, 711490, 712399, 726542, 762959
-
induction of enzyme by high-fat diet, but not by free fatty acids or leptin
distribution of the activity is uneven, being seen mainly in the pericentral rather than the periportal area
-
postnatal day 1, 7 and 14 rats show little or no liver aldehyde oxidase activity. Activity is markedly increased in liver cytosol from rats after postnatal day 14 and is then maintained up to 6 weeks
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AOXB_RAT
1345
0
147872
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
300000
150000
-
native-PAGE/Western blot analysis. Slc:Wistar, Crl:SD, F344/DuCrlCrlj, and Slc:SD strains
300000
-
native-PAGE/Western blot analysis. WKAH/Hkm, WKY/Izm, LEW/CrlCrlj, Crlj:WI, Jcl:Wistar, and Wistar-Imamichi strains
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
-
native-PAGE/Western blot analysis. WKAH/Hkm, WKY/Izm, LEW/CrlCrlj, Crlj:WI, Jcl:Wistar, and Wistar-Imamichi strains
monomer
monomer
-
native-PAGE/Western blot analysis. Slc:Wistar, Crl:SD, F344/DuCrlCrlj, and Slc:SD strains
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
construction of chimeric cDNAs by mutual exchange of 2Fe-2S/FAD and MoCo domains between cynomolgous monkey and rat. Chimeric monkey/rat AO is referred to one with monkey type 2Fe-2S/FAD domains and a rat type MoCo domain. Rat/monkey AO is vice versa. Substrate inhibition is seen in rat AO and chimeric monkey/rat AO, but not in monkey AO and chimeric rat/monkey AO. A biphasic Eadie-Hofstee profile is observed in monkey AO and chimeric rat/monkey AO, but not rat AO and chimeric monkey/rat AO. Two-fold greater Vmax values are observed in monkey AO than in chimeric rat/monkey AO, and in chimeric monkey/rat AO than in rat AO
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1667fold by gel filtration with a yield of 12%, to more than 98% purity
partial purification by heat treatment and ammonium sulfate precipitation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
aldehyde oxidase plays a critical role in nitrite reduction, and this process is regulated by pH, oxygen tension, nitrite, and reducing substrate concentrations
medicine
additional information
medicine
-
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
-
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
-
measurements of NMN and its pyridones usually excreted in the urine can be used to predict the in vivo activity of enzyme
medicine
-
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
-
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
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
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
-
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
-
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
REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maia, L.; Mira, L.
Xanthine oxidase and aldehyde oxidase: A simple procedure for the simultaneous purification from rat liver
Arch. Biochem. Biophys.
400
48-53
2002
Rattus norvegicus
Wroczynski, P.; Wierzchowski, J.
Aromatic aldehydes as fluorogenic indicators for human aldehyde dehydrogenases and oxidases: substrate and isozyme specificity
Analyst
125
511-516
2000
Rattus norvegicus
Wright, R.M.; Clayton, D.A.; Riley, M.G.; McManaman, J.L.; Repine, J.E.
cDNA cloning, sequencing, and characterization of male and female rat liver aldehyde oxidase (rAOX1)
J. Biol. Chem.
274
3878-3886
1999
Rattus norvegicus (Q9Z0U5)
Acheampong, A.A.; Chien, D.S.; Lam, S.; Vekich, S.; Breau, A.; Usansky, J.; Harcourt, D.; Munk, S.A.; Nguyen, H.; Garst, M.; Tang-Liu, D.
Characterization of brimonidine metabolism with rat, rabbit, dog, monkey and human liver fractions and rabbit liver aldehyde oxidase
Xenobiotica
26
1035-1055
1996
Canis lupus familiaris, Oryctolagus cuniculus, Macaca fascicularis, Rattus norvegicus
Tatsumi, K.; Ishigai, M.
Oxime-metabolizing activity of liver aldehyde oxidase
Arch. Biochem. Biophys.
253
413-418
1987
Cavia porcellus, Oryctolagus cuniculus, Mesocricetus auratus, Mus musculus, Rattus norvegicus, Sus scrofa
Kitamura, S.; Tatsumi, K.
Involvement of liver aldehyde oxidase in the reduction of nicotinamide N-oxide
Biochem. Biophys. Res. Commun.
120
602-606
1984
Cavia porcellus, Oryctolagus cuniculus, Mesocricetus auratus, Mus musculus, Rattus norvegicus, Sus scrofa
Stanulovic, M.; Chaykin, S.
Aldehyde oxidase: catalysis of the oxidation of N 1 -methylnicotinamide and pyridoxal
Arch. Biochem. Biophys.
145
27-34
1971
Mus musculus, Rattus norvegicus
Prabhu, R.; Thomas, S.; Balasubramanian, K.A.
Surgical stress-induced alterations in retinoid metabolism in the small intestine: role of oxygen free radicals
Arch. Biochem. Biophys.
434
299-305
2005
Rattus norvegicus
Neumeier, M.; Weigert, J.; Schaeffler, A.; Weiss, T.S.; Schmidl, C.; Buettner, R.; Bollheimer, C.; Aslanidis, C.; Schoelmerich, J.; Buechler, C.
Aldehyde oxidase 1 is highly abundant in hepatic steatosis and is downregulated by adiponectin and fenofibric acid in hepatocytes in vitro
Biochem. Biophys. Res. Commun.
350
731-735
2006
Rattus norvegicus
Klecker, R.W.; Cysyk, R.L.; Collins, J.M.
Zebularine metabolism by aldehyde oxidase in hepatic cytosol from humans, monkeys, dogs, rats, and mice: influence of sex and inhibitors
Bioorg. Med. Chem.
14
62-66
2006
Canis lupus familiaris, Homo sapiens, Macaca fascicularis, Mus musculus, Mus musculus CD-1, Rattus norvegicus
Sasaki, T.; Masubuchi, A.; Yamamura, M.; Watanabe, N.; Hiratsuka, M.; Mizugaki, M.; Itoh, K.; Tanaka, Y.
Rat strain differences in stereospecific 2-oxidation of RS-8359, a reversible and selective MAO-A inhibitor, by aldehyde oxidase
Biopharm. Drug Dispos.
27
247-255
2006
Rattus norvegicus (Q9Z0U5)
Dick, R.A.; Kanne, D.B.; Casida, J.E.
Identification of aldehyde oxidase as the neonicotinoid nitroreductase
Chem. Res. Toxicol.
18
317-323
2005
Gallus gallus, Homo sapiens, Macaca fascicularis, Oryctolagus cuniculus, Rattus norvegicus
Dick, R.A.; Kanne, D.B.; Casida, J.E.
Substrate specificity of rabbit aldehyde oxidase for nitroguanidine and nitromethylene neonicotinoid insecticides
Chem. Res. Toxicol.
19
38-43
2006
Rattus norvegicus
Sugihara, K.; Tayama, Y.; Shimomiya, K.; Yoshimoto, D.; Ohta, S.; Kitamura, S.
Estimation of aldehyde oxidase activity in vivo from conversion ratio of N1-methylnicotinamide to pyridones, and intraspecies variation of the enzyme activity in rats
Drug Metab. Dispos.
34
208-212
2006
Rattus norvegicus
Kundu, T.K.; Hille, R.; Velayutham, M.; Zweier, J.L.
Characterization of superoxide production from aldehyde oxidase: an important source of oxidants in biological tissues
Arch. Biochem. Biophys.
460
113-121
2007
Rattus norvegicus (Q9Z0U5)
Hoshino, K.; Itoh, K.; Masubuchi, A.; Adachi, M.; Asakawa, T.; Watanabe, N.; Kosaka, T.; Tanaka, Y.
Cloning, expression, and characterization of male cynomolgus monkey liver aldehyde oxidase
Biol. Pharm. Bull.
30
1191-1198
2007
Rattus norvegicus, Macaca fascicularis (Q5FB27), Macaca fascicularis
Garattini, E.; Fratelli, M.; Terao, M.
Mammalian aldehyde oxidases: genetics, evolution and biochemistry
Cell. Mol. Life Sci.
65
1019-1048
2008
Arabidopsis thaliana (Q7G191), Arabidopsis thaliana (Q7G192), Arabidopsis thaliana (Q7G193), Bos taurus (P48034), Caenorhabditis elegans (O61198), Caenorhabditis elegans (Q960A1), Canis lupus familiaris (Q2QB47), Canis lupus familiaris (Q2QB48), Danio rerio, Drosophila melanogaster, Drosophila melanogaster (Q9VF53), Equus caballus, Gallus gallus (Q2QB49), Gallus gallus (Q2QB50), Homo sapiens, Macaca fascicularis (Q5FB27), Macaca mulatta, Mamestra brassicae (Q4VGM3), Monodelphis domestica, Mus musculus, Mus musculus (O54754), Mus musculus (Q5SGK3), Mus musculus (Q6V956), Mus musculus (Q8VJ15), no activity in Aspergillus nidulans, Oryctolagus cuniculus (P80456), Pan troglodytes, Pongo pygmaeus, Rattus norvegicus, Rattus norvegicus (Q5QE78), Rattus norvegicus (Q5QE79), Rattus norvegicus (Q5QE80), Rattus norvegicus (Q9Z0U5), Solanum lycopersicum (Q9FV23), Solanum lycopersicum (Q9FV24), Solanum lycopersicum (Q9FV25), Takifugu rubripes, Tetraodon nigroviridis, Xenopus laevis (Q6GMC5), Zea mays (O23887), Zea mays (O23888)
Tayama, Y.; Moriyasu, A.; Sugihara, K.; Ohta, S.; Kitamura, S.
Developmental changes of aldehyde oxidase in postnatal rat liver
Drug Metab. Pharmacokinet.
22
119-124
2007
Rattus norvegicus
Graessler, J.; Fischer, S.
The dual substrate specificity of aldehyde oxidase 1 for retinal and acetaldehyde and its role in ABCA1 mediated efflux
Horm. Metab. Res.
39
775-776
2007
Homo sapiens, Rattus norvegicus, Bos taurus (P48034), Oryctolagus cuniculus (P80456), Gallus gallus (Q2QB50)
Li, H.; Cui, H.; Kundu, T.K.; Alzawahra, W.; Zweier, J.L.
Nitric oxide production from nitrite occurs primarily in tissues not in the blood: critical role of xanthine oxidase and aldehyde oxidase
J. Biol. Chem.
283
17855-17863
2008
Rattus norvegicus
Itoh, K.; Maruyama, H.; Adachi, M.; Hoshino, K.; Watanabe, N.; Tanaka, Y.
Lack of dimer formation ability in rat strains with low aldehyde oxidase activity
Xenobiotica
37
709-716
2007
Rattus norvegicus
Itoh, K.; Adachi, M.; Sato, J.; Shouji, K.; Fukiya, K.; Fujii, K.; Tanaka, Y.
Effects of selenium deficiency on aldehyde oxidase 1 in rats
Biol. Pharm. Bull.
32
190-194
2009
Rattus norvegicus
Itoh, K.; Asakawa, T.; Hoshino, K.; Adachi, M.; Fukiya, K.; Watanabe, N.; Tanaka, Y.
Functional analysis of aldehyde oxidase using expressed chimeric enzyme between monkey and rat
Biol. Pharm. Bull.
32
31-35
2009
Macaca fascicularis, Rattus norvegicus
Kadam, R.; Iyer, K.
Isolation of liver aldehyde oxidase containing fractions from different animals and determination of kinetic parameters for benzaldehyde
Indian J. Pharm. Sci.
70
85-88
2008
Cavia porcellus, Oryctolagus cuniculus, Mus musculus, Rattus norvegicus
Sorouraddin, M.H.; Amini, K.; Naseri, A.; Asgari, D.; Rashidi, M.R.
Study of aldehyde oxidase-catalyzed metabolic pathway of phenanthridine using MCR-ALS method
Bioprocess Biosyst. Eng.
34
173-177
2010
Rattus norvegicus
Li, H.; Kundu, T.K.; Zweier, J.L.
Characterization of the magnitude and mechanism of aldehyde oxidase-mediated nitric oxide production from nitrite
J. Biol. Chem.
284
33850-33858
2009
Rattus norvegicus
Hamzeh-Mivehroud, M.; Rahmani, S.; Rashidi, M.R.; Hosseinpour Feizi, M.A.; Dastmalchi, S.
Structure-based investigation of rat aldehyde oxidase inhibition by flavonoids
Xenobiotica
43
661-670
2013
Rattus norvegicus, Rattus norvegicus SpragueDawley
Zhang, J.W.; Xiao, W.; Gao, Z.T.; Yu, Z.T.; Zhang, J.Y.J.
Metabolism of c-Met kinase inhibitors containing quinoline by aldehyde oxidase, electron donating, and steric hindrance effect
Drug Metab. Dispos.
46
1847-1855
2018
Macaca fascicularis, Homo sapiens, Mus musculus, Rattus norvegicus
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