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
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molybdenum
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allopurinol
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oxidases
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menadione
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benzaldehyde
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abscisic
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n-oxide
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n-heterocyclic
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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
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nitroreduction
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imidacloprid
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neonicotinoids
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phenanthridine
- 1.2.3.1
- xanthine
- molybdenum
- allopurinol
- oxidases
- menadione
- benzaldehyde
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abscisic
- n-oxide
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n-heterocyclic
- moco
- phthalazine
- raloxifene
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molybdenum-containing
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xanthinuria
- hydralazine
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oxidase-mediated
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drug-drug
-
molybdoenzymes
- sulphite
- o6-benzylguanine
- molybdopterin
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flavin-containing
- disulfiram
- n1-methylnicotinamide
- oxypurinol
- nutrition
- medicine
-
hypouricemia
-
amidoxime
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oxidase-catalyzed
- pharmacology
- synthesis
- degradation
- cyp2a6
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nitroreduction
- imidacloprid
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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
Advanced search results
Engineering
Engineering on EC 1.2.3.1 - aldehyde oxidase
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I1085A
slightly higher activity on methotrexate compared to the wild type
I1085A/V1016R
significant decrease in activity compared to the wild type and I1085A mutant
I11085A/A1023Y
catalytic turnover of methotrexate is similar to the I1085A single mutant
A1023Y
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
A1083T
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
A1083T/V1085A
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
I1032V
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
K1004Q
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
K1004Q/K1005R
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
K1004Q/K1005R/M1009I/V1010I
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y/I1032V
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y/I1032V/G1064K/I1067M
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
M1009I
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the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
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
E1265Q
catalytically inactive, residue E1265 initiates the base-catalyzed mechanism of substrate oxidation
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
M884R
drastic decrease in the oxidation of aldehydes, with no increase in the oxidation of purine substrates
V1016F
about 80% decrease in the activity, with a lower molybdenum saturation of around 35%
V806E
drastic decrease in the oxidation of aldehydes, with no increase in the oxidation of purine substrates
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
A1081V
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the mutant completely loses the high cinchonidine oxidation activity of the wild type enzyme
additional information
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plants homozygous for a null allele in AAO4 show a reduction of 30% to 45% in the total levels of benzoic acid in seeds as well as 7% to 9% and 32% to 38% decreases in the levels of 3-benzoyloxypropylglucosinolate and 4-benzoyloxybutylglucosinolate, respectively
additional information
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missense mutations in the coding exons of AOX1, reported in the population of the Churchill County of Nevada and in the Italian population, negatively affect catalytic activity of AOX1
additional information
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mutation of two amino acid residues in the active site of human XOR (mutants E803V and R881M) for purine substrates results in conversion of the substrate preference to aldehyde oxidase type
additional information
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knock-down of isoform AOX1 by siRNA impairs adipogenesis and reduces adiponectin release
additional information
substitution of nucleotides of human AOX1 with relevant ones of rabbit AOX1
additional information
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substitution of nucleotides of human AOX1 with relevant ones of rabbit AOX1
additional information
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construction of chimeric cDNAs by mutual exchange of 2Fe-2S/FAD and MoCo domains between cynomolgous monkey and rat. Chimeric monkey/rat AO is referred to one with monkey type 2Fe-2S/FAD domains and a rat type MoCo domain. Rat/monkey AO is vice versa. Substrate inhibition is seen in rat AO and chimeric monkey/rat AO, but not in monkey AO and chimeric rat/monkey AO. A biphasic EadieHofstee profile is observed in monkey AO and chimeric rat/monkey AO, but not rat AO and chimeric monkey/rat AO. Two-fold greater Vmax values are observed in monkey AO than in chimeric rat/monkey AO, and in chimeric monkey/rat AO than in rat AO
additional information
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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
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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
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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
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construction of chimeric cDNAs by mutual exchange of 2Fe-2S/FAD and MoCo domains between cynomolgous monkey and rat. Chimeric monkey/rat AO is referred to one with monkey type 2Fe-2S/FAD domains and a rat type MoCo domain. Rat/monkey AO is vice versa. Substrate inhibition is seen in rat AO and chimeric monkey/rat AO, but not in monkey AO and chimeric rat/monkey AO. A biphasic Eadie-Hofstee profile is observed in monkey AO and chimeric rat/monkey AO, but not rat AO and chimeric monkey/rat AO. Two-fold greater Vmax values are observed in monkey AO than in chimeric rat/monkey AO, and in chimeric monkey/rat AO than in rat AO