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EC Tree
IUBMB 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].
The taxonomic range for the selected organisms is: Bos taurus 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,
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quinoline oxidase
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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].
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phenanthridine + H2O + O2
6-phenantridone + H2O2
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acetaldehyde + H2O + O2
acetic acid + H2O2
benzaldehyde + H2O + O2
benzoic acid + H2O2
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2,6-dichlorophenol-indophenol also as electron acceptor
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?
butanal + H2O + O2
butyric acid + H2O2
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chloroacetaldehyde + H2O + O2
chloroacetic acid + H2O2
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2,6-dichlorophenol-indophenol as electron acceptor
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crotonaldehyde + H2O + O2
crotonic acid + H2O2
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2,6-dichlorophenol-indophenol as electron acceptor
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?
formaldehyde + H2O + O2
formic acid + H2O2
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2,6-dichlorophenol-indophenol as electron acceptor
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furfural + H2O + O2
2-furoic acid + H2O2
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2,6-dichlorophenol-indophenol as electron acceptor
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hexanal + H2O + O2
hexanoic acid + H2O2
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ir
propionaldehyde + H2O + O2
propionic acid + H2O2
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2,6-dichlorophenol-indophenol as electron acceptor
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?
additional information
?
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acetaldehyde + H2O + O2
acetic acid + H2O2
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acetaldehyde + H2O + O2
acetic acid + H2O2
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2,6-dichlorophenol-indophenol as electron acceptor
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additional information
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enzyme plays an important role in the biotransformation of drugs and xenobiotics, e.g. antiviral, antimalarial and antitumour compounds and nicotine
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additional information
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enzyme plays an important role in the biotransformation of drugs and xenobiotics, e.g. antiviral, antimalarial and antitumour compounds and nicotine
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additional information
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additional information
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enzyme plays an important role in the biotransformation of drugs and xenobiotics, e.g. antiviral, antimalarial and antitumour compounds and nicotine
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?
additional information
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enzyme plays an important role in the biotransformation of drugs and xenobiotics, e.g. antiviral, antimalarial and antitumour compounds and nicotine
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?
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menadione
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complete inhibition at 0.1 mM
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UniProt
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most prominent
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AOX1 is expressed at high levels
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AOX1 is expressed at high levels
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AOX1 is expressed at high levels
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additional information
detectable amounts of enzyme also in eye, kidney, thymus, testis, duodenum, heart and esophagus
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additional information
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detectable amounts of enzyme also in eye, kidney, thymus, testis, duodenum, heart and esophagus
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AOXA_BOVIN
1339
0
147611
Swiss-Prot
other Location (Reliability: 1 )
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150000
alpha2, 2 * 150000, SDS-PAGE
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dimer
alpha2, 2 * 150000, SDS-PAGE
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4°C, 25 mM Tris-HCl buffer, pH 8.2, 19 days, 100% activity retained
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ammonium ions, DTT and FAD protect against inactivation during storage
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Calzi, M.L.; Raviolo, C.; Ghibaudi, E.; de Gioia, L.; Salmona, M.; Cazzaniga, G.; Kurosaki, M.; Terao, M.; Garattini, E.
Purification, cDNA cloning, and tissue distribution of bovine liver aldehyde oxidase
J. Biol. Chem.
270
31037-31045
1995
Bos taurus (P48034), Bos taurus
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Cabre, F.; Canela, E.I.
Purification and properties of bovine liver aldehyde oxidase: comparison with xanthine oxidase
Biochem. Soc. Trans.
15
882-883
1987
Bos taurus
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Takahashi, N.; Sasaki, R.; Chiba, H.
Enzymatic improvement of food flavor IV. Oxidation of aldehydes in soybean extracts by aldehyde oxidase
Agric. Biol. Chem.
43
2557-2561
1979
Bos taurus
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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)
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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)
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