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Information on EC 1.2.3.1 - aldehyde oxidase and Organism(s) Mus musculus and UniProt Accession O54754
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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: Mus musculus
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
AOH1
AOX1
AOX2
mAOX3
quinoline oxidase
-
-
-
-
Retinal oxidase
retinene oxidase
-
-
-
-
Retinal oxidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aldehyde + H2O + O2 = a carboxylate + H2O2
base catalyzed mechanism. Residue E1265 acts as an active site base that abstracts a proton from the Mo-OH group, which in turn undertakes a nucleophilic attack on the substrate benzaldehyde. After hydride transfer to the Mo= S group, the initial intermediate breaks down, with the transient formation of a paramagnetic MoV species, followed by displacement of product by a water molecule to return to the starting LMoVIOS(OH) state. The roles of residues Met884 and Val806 are stabilization of substrate binding
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
2,4-dihydroxybenzaldehyde + H2O + O2
2,4-dihydroxybenzoate + H2O2
-
-
-
?
2-methoxybenzaldehyde + H2O + O2
2-methoxybenzoate + H2O2
-
-
-
?
3-methoxybenzaldehyde + H2O + O2
3-methoxybenzoate + H2O2
-
-
-
?
4-(dimethylamino)cinnamaldehyde + H2O + O2
4-(dimethylamino)cinnamic acid + H2O2
-
-
-
?
4-(dimethylamino)cinnamaldehyde + O2 + H2O
4-(dimethylamine)cinnamate + H2O2
-
-
-
?
4-hydroxybenzaldehyde + H2O + O2
4-hydroxybenzoate + H2O2
-
-
-
?
4-methoxybenzaldehyde + H2O + O2
4-methoxybenzoate + H2O2
-
-
-
?
4-nitrobenzaldehyde + H2O + O2
4-nitrobenzoate + H2O2
-
-
-
?
acetaldehyde + H2O + O2
acetate + H2O2
is a poor substrate of AOX1
-
-
?
all-trans retinaldehyde + H2O + O2
all-trans retinoic acid + H2O2
-
-
-
?
cinnamaldehyde + H2O + O2
cinnamic acid + H2O2
-
-
-
?
crotonaldehyde + H2O + O2
crotonate + H2O2
-
-
-
?
ethyl vanillin + H2O + O2
ethyl vanillic acid + H2O2
-
-
-
?
phenanthridine + H2O + O2
phenanthridinone + H2O2
-
-
-
?
phenylacetaldehyde + H2O + O2
phenylacetic acid + H2O2
-
-
-
?
phenylpropionaldehyde + H2O + O2
phenylpropionic acid + H2O2
-
-
-
?
phthalazine + H2O + O2
1-phthalazinone + H2O2
-
-
-
?
propionaldehyde + H2O + O2
propionic acid + H2O2
-
-
-
?
pyridoxal + H2O + O2
4-pyridoxic acid + H2O2
-
-
-
?
retinalaldehyde + O2 + H2O
retinoic acid + H2O2
-
-
-
?
2,4-dihydroxybenzaldehyde + H2O + O2
2,4-dihydroxybenzoate + H2O2
-
-
-
?
2-methoxybenzaldehyde + H2O + O2
2-methoxybenzoate + 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-methoxybenzaldehyde + H2O + O2
3-methoxybenzoate + H2O2
-
-
-
?
4-(dimethylamino)cinnamaldehyde + H2O + O2
4-(dimethylamino)cinnamic acid + H2O2
-
-
-
?
4-hydroxybenzaldehyde + H2O + O2
4-hydroxybenzoate + H2O2
-
-
-
?
4-methoxybenzaldehyde + H2O + O2
4-methoxybenzoate + H2O2
-
-
-
?
4-nitrobenzaldehyde + H2O + O2
4-nitrobenzoate + 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
-
-
-
-
?
acetaldehyde + H2O + O2
acetate + H2O2
is a poor substrate of AOH1
-
-
?
acetaldehyde + H2O + O2
acetic acid + H2O2
-
-
-
?
allopurinol + H2O + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
benzaldehyde + 2 ferricyanide + H2O
benzoate + 2 ferrocyanide + 2 H+
-
-
-
-
?
benzaldehyde + 2,6-dichlorophenol indophenol
?
natural electron acceptor of enzyme is molecular oxygen, DCPIP i.e., 2,6-dichlorophenol indophenol
-
-
?
benzaldehyde + H2O + 2,6-dichlorophenolindophenol
benzoate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
butanal + 2 ferricyanide + H2O
butanoate + 2 ferrocyanide + 2 H+
-
-
-
-
?
cinnamaldehyde + H2O + O2
cinnamic acid + H2O2
-
-
-
?
crotonaldehyde + H2O + O2
crotonate + H2O2
-
-
-
?
electron donor + nicotinamide N-oxide
nicotinamide + electron acceptor
-
2-hydroxypyrimidine as electron acceptor
-
-
?
ethyl vanillin + H2O + O2
ethyl vanillic acid + H2O2
-
-
-
?
N-[(2-dimethylamino)ethyl] acridine-4-carboxamide + H2O + O2
N-[(2-dimethylamino)ethyl] acridine-4-carboxamide-9(10H)-acridone + H2O2
-
-
-
-
?
N-[2-(dimethylamino)ethyl]acridine-4-carboxamide + H2O + O2
N-[2-(dimethylamino)ethyl]acridine-4-carboxamide-9-(10H)-acridone + H2O2
-
antitumor drug
-
-
?
N1-methyl-nicotineamide + H2O + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N1-methylnicotinamide + 2,6-dichlorophenol indophenol
?
natural electron acceptor of enzyme is molecular oxygen, DCPIP i.e., 2,6-dichlorophenol indophenol
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + H2O2
phenanthridine + H2O + O2
phenanthridinone + H2O2
-
-
-
?
phenylacetaldehyde + H2O + O2
phenylacetic acid + H2O2
-
-
-
?
phenylpropionaldehyde + H2O + O2
phenylpropionic acid + H2O2
-
-
-
?
phthalazine + 2,6-dichlorophenol indophenol
?
natural electron acceptor of enzyme is molecular oxygen, DCPIP i.e., 2,6-dichlorophenol indophenol
-
-
?
phthalazine + H2O + 2,6-dichlorophenol indophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
phthalazine + H2O + O2
1-phthalazinone + H2O2
-
-
-
?
propionaldehyde + H2O + O2
propionic acid + H2O2
-
-
-
?
zebularine + H2O + O2
uridine + H2O2
-
-
major catabolic route for oral antitumor agent zebularine
-
?
acetaldehyde + H2O + O2
acetic acid + H2O2
-
-
-
?
salicylaldehyde + H2O + O2
salicylic acid + H2O2
-
-
-
?
salicylaldehyde + H2O + O2
salicylic acid + H2O2
-
-
-
?
4-(dimethylamino)cinnamaldehyde + O2 + H2O
4-(dimethylamine)cinnamate + H2O2
-
-
-
?
4-(dimethylamino)cinnamaldehyde + O2 + H2O
4-(dimethylamine)cinnamate + H2O2
-
typical substrate spectrum of aldehyde oxidase
-
?
all-trans retinaldehyde + H2O + O2
all-trans retinoic acid + H2O2
AOH1 from the liver of CD1 mice is capable of oxidizing all-trans retinaldehyde
-
-
?
all-trans retinaldehyde + H2O + O2
all-trans retinoic acid + H2O2
AOH2 from the mouse Harderian gland and AOH3 from the mouse Bowman's gland are all capable of oxidizing all-trans retinaldehyde with equal efficiency
-
-
?
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
-
-
-
?
pyridoxal + H2O + O2
4-pyridoxic acid + H2O2
-
-
-
?
retinalaldehyde + O2 + H2O
retinoic acid + H2O2
-
-
-
?
salicylaldehyde + H2O + O2
salicylic acid + H2O2
-
-
-
?
salicylaldehyde + H2O + O2
salicylic acid + 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
?
-
no substrates for isoform AOX1: N1-methylnicotinamide, pyridoxal
-
-
-
additional information
?
-
no substrates for isoform AOX1: N1-methylnicotinamide, pyridoxal
-
-
-
additional information
?
-
no substrates for isoform AOX1: N1-methylnicotinamide, pyridoxal
-
-
-
additional information
?
-
no substrates for isoform AOX1: N1-methylnicotinamide, pyridoxal
-
-
-
additional information
?
-
-
no substrates for isoform AOX1: N1-methylnicotinamide, pyridoxal
-
-
-
additional information
?
-
pyridoxal is not recognized by mouse AOH2
-
-
?
additional information
?
-
pyridoxal is not recognized by mouse AOH2
-
-
?
additional information
?
-
pyridoxal is not recognized by mouse AOH2
-
-
?
additional information
?
-
pyridoxal is not recognized by mouse AOH2
-
-
?
additional information
?
-
no substrate for isoform AOX2: pyridoxal
-
-
-
additional information
?
-
no substrate for isoform AOX2: pyridoxal
-
-
-
additional information
?
-
no substrate for isoform AOX2: pyridoxal
-
-
-
additional information
?
-
no substrate for isoform AOX2: pyridoxal
-
-
-
additional information
?
-
no substrate for isoform AOX3: pyridoxal
-
-
-
additional information
?
-
no substrate for isoform AOX3: pyridoxal
-
-
-
additional information
?
-
no substrate for isoform AOX3: pyridoxal
-
-
-
additional information
?
-
no substrate for isoform AOX3: pyridoxal
-
-
-
additional information
?
-
no substrates for isoform AOX4: N1-methylnicotinamide, pyridoxal
-
-
-
additional information
?
-
no substrates for isoform AOX4: N1-methylnicotinamide, pyridoxal
-
-
-
additional information
?
-
no substrates for isoform AOX4: N1-methylnicotinamide, pyridoxal
-
-
-
additional information
?
-
no substrates for isoform AOX4: N1-methylnicotinamide, pyridoxal
-
-
-
additional information
?
-
-
no substrates for isoform AOX4: N1-methylnicotinamide, pyridoxal
-
-
-
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
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
molybdenum cofactor
purified enzyme displays molybdenum saturation levels around 40%
[2Fe-2S]-center
purified enzyme displays iron saturation levels around 60%
molybdenum cofactor
purified enzyme displays molybdenum saturation levels around 50%
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aspartate
neonatal pretreatment, which reduces circulating growth hormone levels, decreases male aldehyde oxidase activity to female levels
beta-carboline
a far better inhibitor of mouse AOH1 than AOX1
estrogen
reduces liver aldehyde oxidase activity of male animals
glutamate
neonatal pretreatment, which reduces circulating growth hormone levels, decreases male aldehyde oxidase activity to female levels
aspartate
neonatal pretreatment, which reduces circulating growth hormone levels, decreases male aldehyde oxidase activity to female levels
beta-carboline
a far better inhibitor of mouse AOH1 than AOX1
estrogen
reduces liver aldehyde oxidase activity of male animals
fenofibrate
-
in mature adipocytes, enzyme expression is reduced in presence of 50 microM fenofibrate
glutamate
neonatal pretreatment, which reduces circulating growth hormone levels, decreases male aldehyde oxidase activity to female levels
palmitic acid
-
enzyme expression is reduced in 3T3-L1 cells differentiated in presence of 400 microM palmitic acid
menadione
-
0.006 mM, 0.0042 mM, 0.0026 mM, 0.001 mM, 0.0014 mM and 0.0008 mM, 50% inhibition of N-[2-(dimethylamino)ethyl]acridine-4-carboxamide oxidation in male swiss CD mouse, CB57BI/6J, female swiss CD mouse, nude mouse, nude mouse tumor bearing and C129/C57 muse, respectively
additional information
-
activity is significantly reduced by castration of adult males. Hypophysectomy markedly decreases hepatic activity in male and to a lesser extent in female mice
-
additional information
activity is significantly reduced by castration of adult males. Hypophysectomy markedly decreases hepatic activity in male and to a lesser extent in female mice
-
additional information
activity is significantly reduced by castration of adult males. Hypophysectomy markedly decreases hepatic activity in male and to a lesser extent in female mice
-
additional information
activity is significantly reduced by castration of adult males. Hypophysectomy markedly decreases hepatic activity in male and to a lesser extent in female mice
-
additional information
activity is significantly reduced by castration of adult males. Hypophysectomy markedly decreases hepatic activity in male and to a lesser extent in female mice
-
additional information
-
activity is significantly reduced by castration of adult males. Hypophysectomy markedly decreases hepatic activity in male and to a lesser extent in female mice
-
additional information
activity is significantly reduced by castration of adult males. Hypophysectomy markedly decreases hepatic activity in male and to a lesser extent in female mice
-
additional information
activity is significantly reduced by castration of adult males. Hypophysectomy markedly decreases hepatic activity in male and to a lesser extent in female mice
-
additional information
activity is significantly reduced by castration of adult males. Hypophysectomy markedly decreases hepatic activity in male and to a lesser extent in female mice
-
additional information
activity is significantly reduced by castration of adult males. Hypophysectomy markedly decreases hepatic activity in male and to a lesser extent in female mice
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenethyl isothiocyanate
induces AOX1 transcript through a transcriptional mechanism
testosterone
significantly increases activity in castrated males and normal female mice
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0024
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
-
0.0017
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
-
0.001
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
-
0.0024
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
-
0.038
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
-
additional information
additional information
further kinetic parameters of phthalazine-DCPIP reaction in the absence or presence of the inhibitors benzamidine, menadione, norharmane, and raloxifene available in the publication
-
0.0263
2,4-dihydroxybenzaldehyde
wild-type, pH 8.0, 37°C
0.097
2-hydroxypyrimidine
-
apparent Km-value of recombinant mAOX3, pH 7.4, 25°C
0.0008
4-(dimethylamino)cinnamaldehyde
wild-type, pH 8.0, 37°C
0.0019
4-hydroxybenzaldehyde
wild-type, pH 8.0, 37°C
0.0013
4-nitrobenzaldehyde
wild-type, pH 8.0, 37°C
0.133
allopurinol
mutant F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L, pH 8.0,37°C
2.93
allopurinol
mutant F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L, pH 8.0,37°C
2.21
benzaldehyde
mutant F776K/A807E/D878L/L881S/Y885R/P1015T/Y1019L, pH 8.0,37°C
0.011
N-[(2-dimethylamino)ethyl] acridine-4-carboxamide
-
female enzyme treated with testosterone propionate
0.0029
N-[2-(Dimethylamino)ethyl]acridine-4-carboxamide
-
37°C, pH 7.8, strain c129/C57
0.0055
N-[2-(Dimethylamino)ethyl]acridine-4-carboxamide
-
37°C, pH 7.8, nude mouse tumor bearing
0.0074
N-[2-(Dimethylamino)ethyl]acridine-4-carboxamide
-
37°C, pH 7.8, nude mouse
0.027
N-[2-(Dimethylamino)ethyl]acridine-4-carboxamide
-
37°C, pH 7.8, female swiss CD
0.03
N-[2-(Dimethylamino)ethyl]acridine-4-carboxamide
-
37°C, pH 7.8, male swiss CD
0.05
N-[2-(Dimethylamino)ethyl]acridine-4-carboxamide
-
37°C, pH 7.8, strain CB57BI/6J
0.0111
phenylpropionaldehyde
wild-type, pH 8.0, 37°C
0.733
Phthalazine
mutant F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L, pH 8.0,37°C
0.0081
Salicylaldehyde
mutant I1018K, pH 8.0, 37°C
0.0092
Salicylaldehyde
mutant I1018S, pH 8.0, 37°C
0.0136
Salicylaldehyde
mutant M1088V, pH 8.0, 37°C
0.0238
Salicylaldehyde
mutant M1088T, pH 8.0, 37°C
0.0447
Salicylaldehyde
mutant V1016I, pH 8.0, 37°C
0.0559
Salicylaldehyde
mutant V1016L, pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
further kinetic parameters of phthalazine-DCPIP reaction in the absence or presence of the inhibitors benzamidine, menadione, norharmane, and raloxifene available in the publication
-
3.39
2,4-dihydroxybenzaldehyde
wild-type, pH 8.0, 37°C
6.88
2-hydroxypyrimidine
-
apparent Kcat-value of recombinant mAOX3, pH 7.4, 25°C
0.51
4-(dimethylamino)cinnamaldehyde
wild-type, pH 8.0, 37°C
0.53
4-hydroxybenzaldehyde
wild-type, pH 8.0, 37°C
1.22
allopurinol
mutant F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L, pH 8.0,37°C
1.58
allopurinol
mutant F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L, pH 8.0,37°C
3.9
benzaldehyde
mutant F776K/A807E/D878L/L881S/Y885R/P1015T/Y1019L, pH 8.0,37°C
0.53
phenylpropionaldehyde
wild-type, pH 8.0, 37°C
8.73
Phthalazine
mutant F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L, pH 8.0,37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
128
2,4-dihydroxybenzaldehyde
wild-type, pH 8.0, 37°C
605
4-(dimethylamino)cinnamaldehyde
wild-type, pH 8.0, 37°C
0.00008
allopurinol
mutant F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L, pH 8.0,37°C
0.0119
allopurinol
mutant F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L, pH 8.0,37°C
0.0018
benzaldehyde
mutant F776K/A807E/D878L/L881S/Y885R/P1015T/Y1019L, pH 8.0,37°C
46.7
phenylpropionaldehyde
wild-type, pH 8.0, 37°C
0.0119
Phthalazine
mutant F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L, pH 8.0,37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0225
benzamidine
competitive inhibition of phthalazine-2,6-dichlorophenol indophenol reaction, pH 8.0, 37°C
0.00125
menadione
uncompetitive inhibition of phthalazine-2,6-dichlorophenol indophenol reaction, pH 8.0, 37°C
0.018
norharmane
competitive inhibition of phthalazine-2,6-dichlorophenol indophenol reaction, pH 8.0, 37°C
0.0122
raloxifene
competitive inhibition of phthalazine-2,6-dichlorophenol indophenol reaction, pH 8.0, 37°C
0.0591
raloxifene
uncompetitive inhibition of phthalazine-2,6-dichlorophenol indophenol reaction, pH 8.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.026
0.146
substrate salicylaldehyde, pH 8, 37°C, after chemical sulfuration of the molybdopterin cofactor
0.158
substrate salicylaldehyde, pH 8, 37°C, after chemical sulfuration of the molybdopterin cofactor
0.585
substrate salicylaldehyde, pH 8, 37°C, after chemical sulfuration of the molybdopterin cofactor
0.88
substrate salicylaldehyde, pH 8, 37°C, after chemical sulfuration of the molybdopterin cofactor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
AOX1 mRNA is particularly abundant in the epithelial layer
-
preadipocytes have a very low expression of AOX1, in 2 days differentiated cells AOX1 is induced and is not further upregulated in 3, 7 and 9 days differentiated cells. AOX1 mRNA is nearly four-fold higher in 2 days differentiated cells when compared to preadipocytes and doubles from days 2 to 6
richest source of AOH2 mRNA in the adult mouse is the inner ear
-
hepatoma cell line, induction of enzyme isoform AOX1 by 2,3,7,8-tetrachlorodibenzo-p-dioxin
very large amounts of AOH2 are predicted to be present during the early stages of development and specifically in the zygote
additional information
male liver has about 7fold higher content of enzyme than that in female, gender specific regulation in the hepatic tissue
the AOX1 transcript takes time to appear and is measurable only in the fully developed animal
AOH2 and AOH3 mRNAs are expressed in the brain at much lower levels than AOX1 and AOH1
-
-
-
enzyme isoform AOX1 and ite homologue AOH1 are induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin
AOH2 is also present. Aldehyde oxidase activity shows higher levels in male than female adult mice
the AOH1 transcript is already detectable in newborn mice
additional information
-
AOH2 is abundant in the Harderian gland. AOH3 is restricted to the Bowman's gland
additional information
AOH2 is abundant in the Harderian gland. AOH3 is restricted to the Bowman's gland
additional information
AOH2 is abundant in the Harderian gland. AOH3 is restricted to the Bowman's gland
additional information
AOH2 is abundant in the Harderian gland. AOH3 is restricted to the Bowman's gland
additional information
AOH2 is abundant in the Harderian gland. AOH3 is restricted to the Bowman's gland
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enhanced retinal oxidase activity afer exposure to 2,3,7,8-tetrachlorodibenzo-p-dioxin. No effect by supplemental vitamin A
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
isoform AOX1 is the homolog to the human enzyme and produces a rate of approximately 30% of superoxide radicals in relation to moles of substrate converted
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
physiological function
physiological function
-
AOX3 is an enzyme of well known importance in drug metabolism and therefore of increasing importance in recent drug design programs
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). AOXA_MOUSE
1333
0
146678
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
300000
150000
-
SDS-PAGE, native and recombinant protein, degradation products of 130000, 80000, 70000, and 55000 Da in case of purified recombinant mAOX3
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homodimer
each monomer comprises 1335 residues and can be divided into three major domains, a small 20000 Da N-terminal domain that harbors the two FeS clusters and connects to the 40000 Da FAD binding domain and finally the C-terminal 90000 Da domain containing the Moco binding site, with the molybdenum catalytic center
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling. The structures of the isoforms Aox1 to Aox4 are highly preserved and even more conserved than their amino acid sequences. The binding site is composed by a highly conserved region of the Mo center and ligands, and by residues Gln722, Lys889, Arg917 and Ser1085 (mAOX3 numbering), and by a region, which is different among the several isoforms and is located just above the conserved region. The binding site conserved region is also composed by Phe919 (mAOX3 numbering) and by at least one or two hydrophobic residues containing aromatic rings in their side chains (His, Tyr and Phe)
molecular modeling. The structures of the isoforms Aox1 to Aox4 are highly preserved and even more conserved than their amino acid sequences. The binding site is composed by a highly conserved region of the Mo center and ligands, and by residues Gln722, Lys889, Arg917 and Ser1085 (mAOX3 numbering), and by a region, which is different among the several isoforms and is located just above the conserved region. The binding site conserved region is also composed by Phe919 (mAOX3 numbering) and by at least one or two hydrophobic residues containing aromatic rings in their side chains (His, Tyr and Phe). The mAOX1 isoform has the wider specificity region with a variety of polar and charged amino acids
to 2.9 A resolution, used for elucidation of putative reaction mechanism of aldehyde oxidases
vast majority of the crystallization trials performed using the recombinant protein, usable data set of crystals of native mAOX3 with a resolution of 2.9 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E1265Q
catalytically inactive, residue E1265 initiates the base-catalyzed mechanism of substrate oxidation
M884R
drastic decrease in the oxidation of aldehydes, with no increase in the oxidation of purine substrates
V806E
drastic decrease in the oxidation of aldehydes, with no increase in the oxidation of purine substrates
A807V
does not affect the kinetic constants with smaller substrates like benzaldehyde or phthalazine, but affinity for bulkier substrates like phenanthridine decreases, whereas the catalytic efficiency is slightly raised
E1266Q
complete loss of activity with different N-heterocyclic compounds as substrates, 60% reduction of enzyme activity with benzaldehyde
F1014L
amino acid exchange in the active site, 10fold increase in molybdenim content
F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L
all residues in the first coordination sphere around the substrate are exchanged to their counterparts in bovine xanthine oxidoreductase. Mutant shows activity towards benzaldehyde, phthalazine and hypoxanthine
F776K/A807E/D878L/L881S/Y885R/P1015T/Y1019L
all residues in the first coordination sphere around the substrate except K889 are exchanged to their counterparts in bovine xanthine oxidoreductase, mutant is devoid of activity towards most substrates tested, while allopurinnol is oxidized at a low rate
I1018S
KM is decreased 1.5-3fold, while the kcat values overall mainly remain unaffected with all substrates
K889H
23fold decrease in the catalytic efficiency using benzaldehyde and phthalazine as substrates, but the Km-values remain the same
M1088T
the kcat values are significantly increased by about 3fold, mutant displays a lower molybdenum saturation of around 35%
M1088V
the kcat values are reduced to half of the activities of the wild-type enzyme, while the KM values mainly remain unchanged or are also 50% reduced
V1016F
about 80% decrease in the activity, with a lower molybdenum saturation of around 35%
Y885M
kinetic constants remain mainly the same with small hydrophobic substrates like benzaldehyde and phthalazine, bulkier substrates like phenanthridine or more charged substrates like N1-methylnicotinamide are converted with higher efficiency
additional information
additional information
-
AOH2 knock-out mice are viable and transmit the genetic deficit in a mendelian fashion
additional information
AOH2 knock-out mice are viable and transmit the genetic deficit in a mendelian fashion
additional information
AOH2 knock-out mice are viable and transmit the genetic deficit in a mendelian fashion
additional information
AOH2 knock-out mice are viable and transmit the genetic deficit in a mendelian fashion
additional information
AOH2 knock-out mice are viable and transmit the genetic deficit in a mendelian fashion
additional information
-
knock-down of isoform AOX1 by siRNA impairs adipogenesis and reduces adiponectin release
additional information
exchange of several residues in the active site to the ones found in other Aox homologues in mouse or to residues present in bovine xanthine oxidoreductase. Conversion of Aox3 to an xanthine oxidoreductase is achieved exchanging eight residues in the active site. Exchange of the iron-sulfur clusters FeSI, FeSII and both FeSI/FeSII by the corresponding domains of isoform Aox1 results in a decrease in catalytic activity with all substrates tested and both electron acceptor dichlorophenol indophenol and O2
additional information
-
exchange of several residues in the active site to the ones found in other Aox homologues in mouse or to residues present in bovine xanthine oxidoreductase. Conversion of Aox3 to an xanthine oxidoreductase is achieved exchanging eight residues in the active site. Exchange of the iron-sulfur clusters FeSI, FeSII and both FeSI/FeSII by the corresponding domains of isoform Aox1 results in a decrease in catalytic activity with all substrates tested and both electron acceptor dichlorophenol indophenol and O2
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, simplified two-step purification method using Ni-NTA and size-exclusion chromatography
mAOX3 purified from CD1 mouse liver as well as from a heterologous expression system from Escherichia coli, recombinant mAOX3 expressed as an N-terminal fusion protein with a His6 tag
recombinant enzyme, simplified two-step purification method using Ni-NTA and size-exclusion chromatography
recombinant mAOX3 purified using sequential Ni-NTA chromatography and size exclusion chromatography, a chemical sulfuration step performed to further increase the activity of the enzyme 1.4fold and after coexpression with mMCSF and chemical sulfuration, 30% of recombinant mAOX3 exists in the catalytically active form, native mAOX3 purified by ammonium sulfate precipitation with 50% saturation, benzamidine Sepharose chromatography and a linear NaCl gradient on a 5/5 FPLC Mono Q column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA of mAOX3 cloned from mouse CD1 liver into pMMA1 plasmid and expression as an N-terminal fusion protein with a His6 tag, coexpression with mMCSF, heterologous expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens
additional information
-
variations in the levels of aldehyde oxidase activity in different strains of experimental animals
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals
additional information
-
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens
additional information
-
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kishore, G.S.; Boutwell, R.K.
Enzymatic oxidation and reduction of retinal by mouse epidermis
Biochem. Biophys. Res. Commun.
94
1381-1386
1980
Mus musculus
Kurosaki, M.; Demontis, S.; Barzago, M.M.; Garattini, E.; Terao, M.
Molecular cloning of the cDNA coding for mouse aldehyde oxidase: tissue distribution and regulation in vivo by testosterone
Biochem. J.
341
71-80
1999
Mus musculus (O54754), Mus musculus
Yoshihara, S.i.; Tatsumi, K.
Purification and characterization of hepatic aldehyde oxidase in male and female mice
Arch. Biochem. Biophys.
338
29-34
1997
Mus musculus
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
Huang, D.Y.; Furukawa, A.; Ichikawa, Y.
Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in E. coli
Arch. Biochem. Biophys.
364
264-272
1999
Oryctolagus cuniculus, Mus musculus
Al-Salmy, H.S.
Inter-strain variability in aldehyde oxidase activity in the mouse
Comp. Biochem. Physiol. C
132
341-347
2002
Mus musculus
Kurosaki, M.; Terao, M.; Barzago, M.M.; Bastone, A.; Bernardinello, D.; Salmona, M.; Garattini, E.
The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase homologue 3, a novel member of the molybdo-flavoenzyme family with selective expression in the olfactory mucosa
J. Biol. Chem.
279
50482-50498
2004
Mus musculus
Vila, R.; Kurosaki, M.; Barzago, M.M.; Kolek, M.; Bastone, A.; Colombo, L.; Salmona, M.; Terao, M.; Garattini, E.
Regulation and biochemistry of mouse molybdo-flavoenzymes. The DBA/2 mouse is selectively deficient in the expression of aldehyde oxidase homologues 1 and 2 and represents a unique source for the purification and characterization of aldehyde oxidase
J. Biol. Chem.
279
8668-8683
2004
Mus musculus, Mus musculus CD-1, Mus musculus DBA/2
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
Yang, Y.M.; Huang, D.Y.; Liu, G.F.; Zhong, J.C.; Du, K.; Li, Y.F.; Song, X.H.
Effects of 2,3,7,8-tetrachlorodibenzo-p-dioxin on vitamin A metabolism in mice
J. Biochem. Mol. Toxicol.
19
327-335
2005
Mus musculus
Rivera, S.P.; Choi, H.H.; Chapman, B.; Whitekus, M.J.; Terao, M.; Garattini, E.; Hankinson, O.
Identification of aldehyde oxidase 1 and aldehyde oxidase homologue 1 as dioxin-inducible genes
Toxicology
207
401-409
2005
Mus musculus
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)
Weigert, J.; Neumeier, M.; Bauer, S.; Mages, W.; Schnitzbauer, A.A.; Obed, A.; Groeschl, B.; Hartmann, A.; Schaeffler, A.; Aslanidis, C.; Schoelmerich, J.; Buechler, C.
Small-interference RNA-mediated knock-down of aldehyde oxidase 1 in 3T3-L1 cells impairs adipogenesis and adiponectin release
FEBS Lett.
582
2965-2972
2008
Homo sapiens, Mus musculus
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
Schumann, S.; Terao, M.; Garattini, E.; Saggu, M.; Lendzian, F.; Hildebrandt, P.; Leimkuehler, S.
Site directed mutagenesis of amino acid residues at the active site of mouse aldehyde oxidase AOX1
PLoS ONE
4
e5348
2009
Mus musculus (O54754), Mus musculus
Mahro, M.; Coelho, C.; Trincao, J.; Rodrigues, D.; Terao, M.; Garattini, E.; Saggu, M.; Lendzian, F.; Hildebrandt, P.; Romao, M.J.; Leimkuehler, S.
Characterization and crystallization of mouse aldehyde oxidase 3: from mouse liver to Escherichia coli heterologous protein expression
Drug Metab. Dispos.
39
1939-1945
2011
Mus musculus
Coelho, C.; Mahro, M.; Trincao, J.; Carvalho, A.T.; Ramos, M.J.; Terao, M.; Garattini, E.; Leimkuehler, S.; Romao, M.J.
The first mammalian aldehyde oxidase crystal structure: insights into substrate specificity
J. Biol. Chem.
287
40690-40702
2012
Mus musculus (G3X982)
Cerqueira, N.M.; Coelho, C.; Bras, N.F.; Fernandes, P.A.; Garattini, E.; Terao, M.; Romao, M.J.; Ramos, M.J.
Insights into the structural determinants of substrate specificity and activity in mouse aldehyde oxidases
J. Biol. Inorg. Chem.
20
209-217
2015
Mus musculus (Q148T8), Mus musculus (Q5SGK3), Mus musculus (Q8R387), Mus musculus (Q8VI15), Mus musculus
Mahro, M.; Bras, N.F.; Cerqueira, N.M.; Teutloff, C.; Coelho, C.; Romao, M.J.; Leimkuehler, S.
Identification of crucial amino acids in mouse aldehyde oxidase 3 that determine substrate specificity
PLoS ONE
8
e82285
2013
Mus musculus (G3X982), Mus musculus
Kuecuekgoeze, G.; Terao, M.; Garattini, E.; Leimkuehler, S.
Direct comparison of the enzymatic characteristics and superoxide production of the four aldehyde oxidase enzymes present in mouse
Drug Metab. Dispos.
45
947-955
2017
Mus musculus (G3X982), Mus musculus (O54754), Mus musculus (Q3TYQ9), Mus musculus (Q5SGK3), Mus musculus
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
Kuecuekgoeze, G.; Leimkuehler, S.
Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities
PLoS ONE
13
e0191819
2018
Mus musculus (G3X982), Mus musculus (O54754), Mus musculus (Q3TYQ9), Mus musculus (Q5SGK3), Mus musculus
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