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Literature summary for 1.2.3.1 extracted from

  • 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 (2011), Drug Metab. Dispos., 39, 1939-1945.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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 Mus musculus

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
benzaldehyde apparent Km-value of native mAOX3, pH 7.4, 25°C Mus musculus
0.02
-
benzaldehyde apparent Km-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
0.026
-
Butanal apparent Km-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
0.029
-
Butanal apparent Km-value of native mAOX3, pH 7.4, 25°C Mus musculus
0.097
-
2-hydroxypyrimidine apparent Km-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
0.173
-
2-hydroxypyrimidine apparent Km-value of native mAOX3, pH 7.4, 25°C Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
SDS-PAGE, native and recombinant protein, degradation products of 130000, 80000, 70000, and 55000 Da in case of purified recombinant mAOX3 Mus musculus
300000
-
gel filtration, native and recombinant mAOX3 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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 Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxypyrimidine + H2O + ferricyanide + O2
-
Mus musculus ?
-
?
benzaldehyde + 2 ferricyanide + H2O
-
Mus musculus benzoate + 2 ferrocyanide + 2 H+
-
?
butanal + 2 ferricyanide + H2O
-
Mus musculus butanoate + 2 ferrocyanide + 2 H+
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 150000, gel filtration Mus musculus

Synonyms

Synonyms Comment Organism
mAOX3
-
Mus musculus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.733
-
benzaldehyde apparent Kcat-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
2.167
-
benzaldehyde apparent Kcat-value of native mAOX3, pH 7.4, 25°C Mus musculus
2.333
-
Butanal apparent Kcat-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
6.4
-
Butanal apparent Kcat-value of native mAOX3, pH 7.4, 25°C Mus musculus
6.88
-
2-hydroxypyrimidine apparent Kcat-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
21.32
-
2-hydroxypyrimidine apparent Kcat-value of native mAOX3, pH 7.4, 25°C Mus musculus

Cofactor

Cofactor Comment Organism Structure
FAD
-
Mus musculus
molybdenum cofactor i.e. MoCo Mus musculus
[2Fe-2S]-center two distinct ones Mus musculus

General Information

General Information Comment Organism
physiological function AOX3 is an enzyme of well known importance in drug metabolism and therefore of increasing importance in recent drug design programs Mus musculus