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Information on EC 1.2.3.1 - aldehyde oxidase and Organism(s) Zea mays and UniProt Accession O23887
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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: Zea mays
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
benzaldehyde + H2O + O2
benzoic acid + H2O2
-
2,6-dichlorophenol-indophenol also as electron acceptor
-
-
?
indole 3-acetaldehyde + H2O + O2
indole 3-acetic acid + H2O2
-
2,6-dichlorophenol-indophenol also as electron acceptor
-
-
?
indole 3-carbaldehyde + H2O + O2
indole 3-carboxylate + H2O2
-
2,6-dichlorophenol-indophenol also as electron acceptor
-
-
?
phenylacetaldehyde + H2O + O2
phenylacetic acid + H2O2
-
2,6-dichlorophenol-indophenol as electron acceptor
-
-
?
protocatechualdehyde + H2O + O2
protocatechuic acid + H2O2
-
2,6-dichlorophenol-indophenol also as electron acceptor
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koshiba, T.; Saito, E.; Ono, N.; Yamamoto, N.; Sato, M.
Purification and properties of flavin- and molybdenum-containing aldehyde oxidase from coleoptiles of maize
Plant Physiol.
110
781-789
1996
Zea mays
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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