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(S)-RS-8359 + H2O + O2
2-keto-(S)-RS-8359 + H2O2
benzaldehyde + H2O + O2
benzoate + H2O2
-
-
-
?
imidacloprid + H2O + O2 + N-methylnicotinamide
nitroso-imidacloprid + amino-imidacloprid + H2O2 + ?
-
-
-
?
methotrexate + H2O + O2
?
-
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + H2O2
p-dimethyl aminocinnamaldehyde + H2O + O2
? + H2O2
-
-
-
?
(S)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine + H2O + O2
? + H2O2
-
i.e. S-8359
-
-
?
(S)-RS-8359 + H2O + O2
2-keto-(S)-RS-8359 + H2O2
Donryu rats show a dimorphic pattern for the 2-oxidation activity of RS-8359
-
-
?
1-methoxy-2-naphthaldehyde + H2O + O2
1-methoxy-2-naphthoic acid + H2O2
-
-
-
-
?
2-naphthaldehyde + H2O + O2
2-naphthoic acid + 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 brimonidine + 4 H2O + 4 O2
2-oxobrimonidine + 3-oxobrimonidine + 2,3-dioxobrimonidine + 4 H2O2
-
-
-
-
?
3-methoxy-2-naphthaldehyde + H2O + O2
3-methoxy-2-naphthoic acid + H2O2
-
-
-
-
?
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine + H2O + O2
? + H2O2
-
i.e. RS-8359, 2-oxidation of the S-enantiomer
-
-
?
4-(dimethylamino)-cinnamaldehyde + H2O + O2
?
-
-
-
-
?
4-(dimethylamino)cinnamaldehyde + H2O + O2
?
-
-
-
-
?
4-(dimethylamino)cinnamaldehyde + nitrite + H2O + O2
? + nitric oxide
-
in the presence of typical aldehyde substrates like 4-(dimethylamino)cinnamaldehyde or NADH, aldehyde oxidase reduces nitrite to nitric oxide
-
-
?
6-dimethyloamino-2-naphthaldehyde + H2O + O2
6-dimethylamino-2-naphthoic acid + H2O2
-
-
-
-
?
6-methoxy-2-naphthaldehyde + H2O + O2
6-methoxy-2-naphthoic acid + 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
-
-
-
-
?
7-methoxy-1-naphthaldehyde + H2O + O2
7-methoxy-2-naphthoic acid + H2O2
-
-
-
-
?
acetophenone oxime + H2O + 2-hydroxypyrimidine
acetophenone + NH3
-
-
-
-
?
anthracene-9-carboxaldehyde + H2O + O2
anthracene-9-carboxylate + H2O2
-
-
-
-
?
benzaldehyde + 2 ferricyanide + H2O
benzoate + 2 ferrocyanide + 2 H+
-
-
-
-
?
benzaldehyde + H2O + O2
benzoate + H2O2
clothianidin + NMNH
nitroso-clothianidin + amino-clothianidin + ?
-
-
-
-
?
electron donor + nicotinamide N-oxide
nicotinamide + electron acceptor
-
2-hydroxypyrimidine as electron acceptor
-
-
?
imidacloprid + H2O + O2 + N-methylnicotinamide
nitroso-imidacloprid + amino-imidacloprid + H2O2 + ?
-
-
in presence of N-methylnicotinamide, ratio of amino- to nitroso-products is 23 to 14
-
?
imidacloprid + NMNH
nitroso-imidacloprid + amino-imidacloprid + ?
-
-
-
-
?
methotrexate + H2O + O2
7-hydroxymethotrexate + H2O2
-
-
-
-
?
methotrexate + H2O + O2
?
-
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + ?
-
variations in the ratio of the amount of pyridones to the total amount of NMN and pyridones in urine are closely related to the enzyme activity
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + H2O2
NADH + nitrite + H2O + O2
? + nitric oxide
-
in the presence of typical aldehyde substrates like 4-(dimethylamino)cinnamaldehyde or NADH, aldehyde oxidase reduces nitrite to nitric oxide. NADH reacts with aldehyde oxidase at the FAD site of the enzyme
-
-
?
nitenpyram + NMNH
nitroso-nitenpyram + amino-nitenpyram + ?
-
-
-
-
?
phenanthrene-9-carboxaldehyde + H2O + O2
phenanthrene-9-carboxylate + H2O2
-
-
-
-
?
phenanthridine + H2O + O2
?
-
inhibitory effects of 15 flavonoids on the activity of rat liver aldehyde oxidase assessed, glycosylated flavonoids show relatively weaker inhibition, quantitative structureactivity relationship studies performed to elucidate the important structural properties responsible for the observed inhibitory effects
-
-
?
phenanthridine + H2O + O2
phenanthridinone + H2O2
-
-
-
-
?
pyridoxal + H2O + O2
4-pyridoxic acid + H2O2
-
-
-
-
?
vanillin + H2O + O2
vanillic acid + H2O2
-
-
-
-
?
zebularine + H2O + O2
uridine + H2O2
-
-
major catabolic route for oral antitumor agent zebularine
-
?
additional information
?
-
(S)-RS-8359 + H2O + O2
2-keto-(S)-RS-8359 + H2O2
i.e. 4-([(7S)-7-hydroxy-6,7-dihydro-5H-cyclopenta[d]pyrimidin-4-yl]amino)benzonitrile, reversible inhibitor of monoamine oxidase A. Remarkable strain differences in activity on substrate, correlating in part with expressed levels of protein
-
-
?
(S)-RS-8359 + H2O + O2
2-keto-(S)-RS-8359 + H2O2
Donryu rats show a dimorphic pattern for the 2-oxidation activity of RS-8359
-
-
?
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
-
-
-
?
(S)-RS-8359
?
-
-
-
-
?
(S)-RS-8359
?
-
enzyme shows a monophasic pattern in Eadie-Hofstee plots of the (S)-enantiospecific 2-oxidation activity of RS-8359
-
-
?
benzaldehyde + H2O + O2
benzoate + H2O2
-
-
-
?
benzaldehyde + H2O + O2
benzoate + H2O2
-
-
-
-
?
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
-
-
-
?
N1-methylnicotinamide + H2O + O2
N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + 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 is of interest as a source of the reactive oxygen species, hydrogen peroxide and the superoxide anion
-
-
?
additional information
?
-
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
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
?
-
-
a wide variety of xenobiotics may serve as electron acceptors instead of molecular oxygen. Enzyme reduces nitroguanidines to both nitroso- and aminoguanidines, while nitromethylens are reduced only to the corrsponding nitroso metabolites. Reduction of nitroguanidines to amino metabolites depends on enzyme concentration
-
-
?
additional information
?
-
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
low and negligible quinine-oxidizing activity
-
-
?
additional information
?
-
-
phenanthridine N-oxide is not metabolized by the enzyme
-
-
?
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0.0804 - 0.173
(S)-RS-8359
0.355 - 1.895
N-methylnicotinamide
0.0341 - 0.0407
(S)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
0.0055
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
-
0.0043 - 0.0528
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
0.0096
4-(dimethylamino)cinnamaldehyde
-
in the presence of 1 mM nitrite, at pH 6.0 and 37°C
0.001
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
-
0.0011
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
-
0.004
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
-
0.064
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
-
0.052 - 1.03
clothianidin
0.024
NADH
-
in the presence of 1 mM nitrite, at pH 6.0 and 37°C
0.0804
(S)-RS-8359
pH 7.4, 37°C, enzyme from Wistar-Imamichi strain, ratio Vmax/Km 1.98 microl per min and mg
0.0813
(S)-RS-8359
pH 7.4, 37°C, enzyme from Jcl:Wistar strain, ratio Vmax/Km 1.00 microl per min and mg
0.0833
(S)-RS-8359
pH 7.4, 37°C, enzyme from Crj:Wistar strain, ratio Vmax/Km 1.46 microl per min and mg
0.1046
(S)-RS-8359
pH 7.4, 37°C, enzyme from LEW:Crj strain, ratio Vmax/Km 0.58 microl per min and mg
0.14
(S)-RS-8359
pH 7.4, 37°C, enzyme from F344/DuCrj strain, ratio Vmax/Km 0.01 microl per min and mg
0.17
(S)-RS-8359
pH 7.4, 37°C, enzyme from Slc:SD strain, ratio Vmax/Km 0.09 microl per min and mg
0.173
(S)-RS-8359
pH 7.4, 37°C, enzyme from Crj:SD strain, ratio Vmax/Km 0.06 microl per min and mg
0.355
N-methylnicotinamide
female rat liver enzyme after reduction with DTT
0.36
N-methylnicotinamide
male rat liver enzyme after reduction with DTT
0.538
N-methylnicotinamide
male rat liver enzyme
1.063
N-methylnicotinamide
female rat liver enzyme
1.895
N-methylnicotinamide
female rat liver enzyme after reduction with DTT and reoxidation with 4,4'-dithiodipyridine
0.0341
(S)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
pH 7.4, 37°C
0.0407
(S)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
pH 7.4, 37°C, enzyme isolated from animals fed with a selenium-deficient diet
0.0043
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
chimeric rat/monkey enzyme, high affinity value, pH 6.0, 37°C
0.0171
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
chimeric rat/monkey enzyme, low affinity value, pH 6.0, 37°C
0.0363
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
chimeric monkey/rat enzyme, pH 6.0, 37°C
0.0528
4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine
-
wild-type, pH 6.0, 37°C
0.052
clothianidin
-
aminoguanidine formation, pH 7.4, 37°C
1.03
clothianidin
-
nitrosoguanidine formation, pH 7.4, 37°C
0.16
imidacloprid
-
aminoguanidine formation, pH 7.4, 37°C
2.99
imidacloprid
-
nitrosoguanidine formation, pH 7.4, 37°C
0.084
nitenpyram
-
aminoguanidine formation, pH 7.4, 37°C
2.41
nitenpyram
-
nitrosoguanidine formation, pH 7.4, 37°C
2.7
nitrite
-
in the presence of 0.1 mM NADH, at pH 6.0 and 37°C
3.3
nitrite
-
in the presence of 0.05 mM 4-(dimethylamino)cinnamaldehyde, at pH 6.0 and 37°C
0.014
Vanillin
-
pH 7.4, 37°C
0.0158
Vanillin
-
pH 7.4, 37°C, enzyme isolated from animals fed with a selenium-deficient diet
0.011
zebularine
-
female, pH 7.5, 37°C
0.011
zebularine
-
male, pH 7.5, 37°C
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medicine
aldehyde oxidase can be an important basal source of superoxide that will be enhanced in disease settings where cellular aldehyde levels are increased
degradation
-
aldehyde oxidase plays a critical role in nitrite reduction, and this process is regulated by pH, oxygen tension, nitrite, and reducing substrate concentrations
medicine
-
surgical stress model of oxidative stress in retinoid metabolism, prevention of alterations in enzyme activity and alkaline phosphatase activity by inhibition of superoxide generation using allopurinol
medicine
-
adiponectin and fenobibric acid reduce enzyme isoform AOX1 by activating peroxisome proliferator-activated receptor alpha whereas fatty liver disease is associated with elevated hepatic AOX1 level
medicine
-
measurements of NMN and its pyridones usually excreted in the urine can be used to predict the in vivo activity of enzyme
medicine
-
aldehyde oxidase activity in rats estimated on the basis of benzaldehyde, N1-methylnicotinamide and methotrexate oxidase activities rapidly increases from birth, reaching a plateau within 4 weeks, and is regulated by expression of the protein. Aldehyde oxidase plays an important role in metabolizing many drugs that may be administered to pediatric patients. Developmental changes are important for the clinical application in infants of methotrexate and other drugs that are detoxified by aldehyde oxidase
medicine
-
3-substituted quinoline triazolopyridine compounds used as c-Met kinase inhibitors are subject to aldehyde oxidase-mediated metabolism. Several compouinds 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
additional information
-
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
-
rat strains with low aldehyde oxidase activity show only a monomer, whereas strains with high activity overwhelmingly exhibit a dimer. Expression levels of aldehyde oxidase homodimer are primarily responsible for rat strain differences in aldehyde oxidase activity
additional information
-
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
additional information
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme
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Maia, L.; Mira, L.
Xanthine oxidase and aldehyde oxidase: A simple procedure for the simultaneous purification from rat liver
Arch. Biochem. Biophys.
400
48-53
2002
Rattus norvegicus
brenda
Wroczynski, P.; Wierzchowski, J.
Aromatic aldehydes as fluorogenic indicators for human aldehyde dehydrogenases and oxidases: substrate and isozyme specificity
Analyst
125
511-516
2000
Rattus norvegicus
brenda
Wright, R.M.; Clayton, D.A.; Riley, M.G.; McManaman, J.L.; Repine, J.E.
cDNA cloning, sequencing, and characterization of male and female rat liver aldehyde oxidase (rAOX1)
J. Biol. Chem.
274
3878-3886
1999
Rattus norvegicus (Q9Z0U5)
brenda
Acheampong, A.A.; Chien, D.S.; Lam, S.; Vekich, S.; Breau, A.; Usansky, J.; Harcourt, D.; Munk, S.A.; Nguyen, H.; Garst, M.; Tang-Liu, D.
Characterization of brimonidine metabolism with rat, rabbit, dog, monkey and human liver fractions and rabbit liver aldehyde oxidase
Xenobiotica
26
1035-1055
1996
Canis lupus familiaris, Oryctolagus cuniculus, Macaca fascicularis, Rattus norvegicus
brenda
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
brenda
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
brenda
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
brenda
Prabhu, R.; Thomas, S.; Balasubramanian, K.A.
Surgical stress-induced alterations in retinoid metabolism in the small intestine: role of oxygen free radicals
Arch. Biochem. Biophys.
434
299-305
2005
Rattus norvegicus
brenda
Neumeier, M.; Weigert, J.; Schaeffler, A.; Weiss, T.S.; Schmidl, C.; Buettner, R.; Bollheimer, C.; Aslanidis, C.; Schoelmerich, J.; Buechler, C.
Aldehyde oxidase 1 is highly abundant in hepatic steatosis and is downregulated by adiponectin and fenofibric acid in hepatocytes in vitro
Biochem. Biophys. Res. Commun.
350
731-735
2006
Rattus norvegicus
brenda
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
brenda
Sasaki, T.; Masubuchi, A.; Yamamura, M.; Watanabe, N.; Hiratsuka, M.; Mizugaki, M.; Itoh, K.; Tanaka, Y.
Rat strain differences in stereospecific 2-oxidation of RS-8359, a reversible and selective MAO-A inhibitor, by aldehyde oxidase
Biopharm. Drug Dispos.
27
247-255
2006
Rattus norvegicus (Q9Z0U5)
brenda
Dick, R.A.; Kanne, D.B.; Casida, J.E.
Identification of aldehyde oxidase as the neonicotinoid nitroreductase
Chem. Res. Toxicol.
18
317-323
2005
Gallus gallus, Homo sapiens, Macaca fascicularis, Oryctolagus cuniculus, Rattus norvegicus
brenda
Dick, R.A.; Kanne, D.B.; Casida, J.E.
Substrate specificity of rabbit aldehyde oxidase for nitroguanidine and nitromethylene neonicotinoid insecticides
Chem. Res. Toxicol.
19
38-43
2006
Rattus norvegicus
brenda
Sugihara, K.; Tayama, Y.; Shimomiya, K.; Yoshimoto, D.; Ohta, S.; Kitamura, S.
Estimation of aldehyde oxidase activity in vivo from conversion ratio of N1-methylnicotinamide to pyridones, and intraspecies variation of the enzyme activity in rats
Drug Metab. Dispos.
34
208-212
2006
Rattus norvegicus
brenda
Kundu, T.K.; Hille, R.; Velayutham, M.; Zweier, J.L.
Characterization of superoxide production from aldehyde oxidase: an important source of oxidants in biological tissues
Arch. Biochem. Biophys.
460
113-121
2007
Rattus norvegicus (Q9Z0U5)
brenda
Hoshino, K.; Itoh, K.; Masubuchi, A.; Adachi, M.; Asakawa, T.; Watanabe, N.; Kosaka, T.; Tanaka, Y.
Cloning, expression, and characterization of male cynomolgus monkey liver aldehyde oxidase
Biol. Pharm. Bull.
30
1191-1198
2007
Rattus norvegicus, Macaca fascicularis (Q5FB27), Macaca fascicularis
brenda
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)
brenda
Tayama, Y.; Moriyasu, A.; Sugihara, K.; Ohta, S.; Kitamura, S.
Developmental changes of aldehyde oxidase in postnatal rat liver
Drug Metab. Pharmacokinet.
22
119-124
2007
Rattus norvegicus
brenda
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)
brenda
Li, H.; Cui, H.; Kundu, T.K.; Alzawahra, W.; Zweier, J.L.
Nitric oxide production from nitrite occurs primarily in tissues not in the blood: critical role of xanthine oxidase and aldehyde oxidase
J. Biol. Chem.
283
17855-17863
2008
Rattus norvegicus
brenda
Itoh, K.; Maruyama, H.; Adachi, M.; Hoshino, K.; Watanabe, N.; Tanaka, Y.
Lack of dimer formation ability in rat strains with low aldehyde oxidase activity
Xenobiotica
37
709-716
2007
Rattus norvegicus
brenda
Itoh, K.; Adachi, M.; Sato, J.; Shouji, K.; Fukiya, K.; Fujii, K.; Tanaka, Y.
Effects of selenium deficiency on aldehyde oxidase 1 in rats
Biol. Pharm. Bull.
32
190-194
2009
Rattus norvegicus
brenda
Itoh, K.; Asakawa, T.; Hoshino, K.; Adachi, M.; Fukiya, K.; Watanabe, N.; Tanaka, Y.
Functional analysis of aldehyde oxidase using expressed chimeric enzyme between monkey and rat
Biol. Pharm. Bull.
32
31-35
2009
Macaca fascicularis, Rattus norvegicus
brenda
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
brenda
Sorouraddin, M.H.; Amini, K.; Naseri, A.; Asgari, D.; Rashidi, M.R.
Study of aldehyde oxidase-catalyzed metabolic pathway of phenanthridine using MCR-ALS method
Bioprocess Biosyst. Eng.
34
173-177
2010
Rattus norvegicus
brenda
Li, H.; Kundu, T.K.; Zweier, J.L.
Characterization of the magnitude and mechanism of aldehyde oxidase-mediated nitric oxide production from nitrite
J. Biol. Chem.
284
33850-33858
2009
Rattus norvegicus
brenda
Hamzeh-Mivehroud, M.; Rahmani, S.; Rashidi, M.R.; Hosseinpour Feizi, M.A.; Dastmalchi, S.
Structure-based investigation of rat aldehyde oxidase inhibition by flavonoids
Xenobiotica
43
661-670
2013
Rattus norvegicus, Rattus norvegicus SpragueDawley
brenda
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
brenda