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
-
molybdenum
-
allopurinol
-
oxidases
-
menadione
-
benzaldehyde
-
abscisic
-
n-oxide
-
n-heterocyclic
-
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
-
nitroreduction
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imidacloprid
-
neonicotinoids
-
phenanthridine
- 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
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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Cofactor
Cofactor on EC 1.2.3.1 - aldehyde oxidase
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NAD+
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enzyme is able to oxidize benzaldehyde without NAD+, but its activity increases by 50% when the cofactor is added. Km value 0.0581 mM
[4Fe-4S]-center
Q84IX9; Q84IY0 andQ84IX8
presence of a [4Fe-4 S] cluster in the medium subunit
molybdenum cofactor
during the displacement of the products away from the Moco, the transfer of electrons from the catalytic site to the FAD site is proton-coupled. The most favorable and fastest pathway for the enzyme to complete its catalytic cycle is that with MoV and a deprotonated SH ligand of the Moco with the FAD molecule converted to its semiquinone form, FADH radical
molybdenum cofactor
protein contains a molybdenum cofactor-binding domain
molybdenum cofactor
purified enzyme displays molybdenum saturation levels around 40%
molybdenum cofactor
purified enzyme displays molybdenum saturation levels around 50%
[2Fe-2S]-center
protein contains 2 2Fe-2S iron-sulfur-cluster-binding domains
[2Fe-2S]-center
purified enzyme displays iron saturation levels around 60%