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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

Reaction

an aldehyde
+
H2O
 +
O2
=
a carboxylate
 +
H2O2

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

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.3 With oxygen as acceptor
                1.2.3.1 aldehyde oxidase

Engineering

Engineering on EC 1.2.3.1 - aldehyde oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A1023Y
significant decrease in activity on methotrexate
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
V1016R
significant decrease in activity on methotrexate
A1023Y
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme
V1085A
-
the mutant acquires high cinchonidine oxidation activity
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
F1014I
amino acid exchange in the active site
F1014L
amino acid exchange in the active site, 10fold increase in molybdenim content
F1014V
amino acid exchange in the active site
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
I1018K
activities roughly similar to wild-type
I1018S
KM is decreased 1.5-3fold, while the kcat values overall mainly remain unaffected with all substrates
K889H
2–3fold 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
P1015A
amino acid exchange in the active site
P1015G
amino acid exchange in the active site
V1016F
about 80% decrease in the activity, with a lower molybdenum saturation of around 35%
V1016I
about 80% decrease in the activity
V1016L
about 80% decrease in the activity
V806E
drastic decrease in the oxidation of aldehydes, with no increase in the oxidation of purine substrates
V806E/M884R
catalytically inactive
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
-
the mutant completely loses the high cinchonidine oxidation activity of the wild type enzyme
additional information