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Information on EC 1.2.3.1 - aldehyde oxidase and Organism(s) Bos taurus and UniProt Accession P48034

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EC Tree
     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.3 With oxygen as acceptor
                1.2.3.1 aldehyde oxidase
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].
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Bos taurus
UNIPROT: P48034
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
aldehyde oxidase, aldehyde oxidase 1, retinal oxidase, formate oxidase, maox3, atraaox2, aldehyde oxidase 3, aldehyde oxidase 2, aldehyde:oxygen oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldehyde oxidase 1
-
AOX
-
-
quinoline oxidase
-
-
-
-
Retinal oxidase
-
-
-
-
retinene oxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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 hide
9029-07-6
-
9033-52-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phenanthridine + H2O + O2
6-phenantridone + H2O2
show the reaction diagram
-
-
-
?
acetaldehyde + H2O + O2
acetic acid + H2O2
show the reaction diagram
benzaldehyde + H2O + O2
benzoic acid + H2O2
show the reaction diagram
-
2,6-dichlorophenol-indophenol also as electron acceptor
-
-
?
butanal + H2O + O2
butyric acid + H2O2
show the reaction diagram
-
-
-
-
?
chloroacetaldehyde + H2O + O2
chloroacetic acid + H2O2
show the reaction diagram
-
2,6-dichlorophenol-indophenol as electron acceptor
-
-
?
crotonaldehyde + H2O + O2
crotonic acid + H2O2
show the reaction diagram
-
2,6-dichlorophenol-indophenol as electron acceptor
-
-
?
formaldehyde + H2O + O2
formic acid + H2O2
show the reaction diagram
-
2,6-dichlorophenol-indophenol as electron acceptor
-
-
?
furfural + H2O + O2
2-furoic acid + H2O2
show the reaction diagram
-
2,6-dichlorophenol-indophenol as electron acceptor
-
-
?
hexanal + H2O + O2
hexanoic acid + H2O2
show the reaction diagram
-
-
-
-
ir
propionaldehyde + H2O + O2
propionic acid + H2O2
show the reaction diagram
-
2,6-dichlorophenol-indophenol as electron acceptor
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdopterin
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
menadione
-
menadione
-
complete inhibition at 0.1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AOXA_BOVIN
1339
0
147611
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
alpha2, 2 * 150000, SDS-PAGE
300000
gel filtration
222000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
alpha2, 2 * 150000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 25 mM Tris-HCl buffer, pH 8.2, 19 days, 100% activity retained
-
ammonium ions, DTT and FAD protect against inactivation during storage
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team