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Literature summary for 1.2.3.1 extracted from

  • 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 (2009), PLoS ONE, 4, e5348.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mus musculus

Protein Variants

Protein Variants Comment Organism
E1265Q catalytically inactive, residue E1265 initiates the base-catalyzed mechanism of substrate oxidation Mus musculus
M884R drastic decrease in the oxidation of aldehydes, with no increase in the oxidation of purine substrates Mus musculus
V806E drastic decrease in the oxidation of aldehydes, with no increase in the oxidation of purine substrates Mus musculus
V806E/M884R catalytically inactive Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0075
-
retinaldehyde mutant M884R, 30°C, pH 7.4 Mus musculus
0.0114
-
Phthalazine wild-type, 30°C, pH 7.4 Mus musculus
0.0222
-
retinaldehyde mutant V806E, 30°C, pH 7.4 Mus musculus
0.0285
-
Phthalazine mutant V806E, 30°C, pH 7.4 Mus musculus
0.0558
-
retinaldehyde wild-type, 30°C, pH 7.4 Mus musculus
0.0977
-
benzaldehyde wild-type, 30°C, pH 7.4 Mus musculus
0.5199
-
acetaldehyde wild-type, 30°C, pH 7.4 Mus musculus
0.6345
-
benzaldehyde mutant V806E, 30°C, pH 7.4 Mus musculus
7.13
-
benzaldehyde mutant M884R, 30°C, pH 7.4 Mus musculus
52.9
-
acetaldehyde mutant V806E, 30°C, pH 7.4 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus O54754
-
-

Reaction

Reaction Comment Organism Reaction ID
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 Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + H2O + O2
-
Mus musculus acetic acid + H2O2
-
?
benzaldehyde + H2O + O2
-
Mus musculus benzoate + H2O2
-
?
additional information no substrate: xanthine, hypoxanthine Mus musculus ?
-
?
phthalazine + H2O + O2
-
Mus musculus ? + H2O2
-
?
retinaldehyde + O2 + H2O
-
Mus musculus retinoic acid + H2O2
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.022
-
retinaldehyde mutant M884R, 30°C, pH 7.4 Mus musculus
0.19
-
Phthalazine wild-type, 30°C, pH 7.4 Mus musculus
0.23
-
retinaldehyde mutant V806E, 30°C, pH 7.4 Mus musculus
0.83
-
retinaldehyde wild-type, 30°C, pH 7.4 Mus musculus
1.27
-
benzaldehyde mutant M884R, 30°C, pH 7.4 Mus musculus
1.72
-
Phthalazine mutant V806E, 30°C, pH 7.4 Mus musculus
2.52
-
benzaldehyde mutant V806E, 30°C, pH 7.4 Mus musculus
2.7
-
acetaldehyde mutant V806E, 30°C, pH 7.4 Mus musculus
5.29
-
benzaldehyde wild-type, 30°C, pH 7.4 Mus musculus
8.66
-
acetaldehyde wild-type, 30°C, pH 7.4 Mus musculus