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Literature summary 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)

EC Number Cloned (Comment) Organism
1.2.3.1 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)

EC Number Crystallization (Comment) Organism
1.2.3.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.3.1 0.013
-
benzaldehyde apparent Km-value of native mAOX3, pH 7.4, 25°C Mus musculus
1.2.3.1 0.02
-
benzaldehyde apparent Km-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
1.2.3.1 0.026
-
Butanal apparent Km-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
1.2.3.1 0.029
-
Butanal apparent Km-value of native mAOX3, pH 7.4, 25°C Mus musculus
1.2.3.1 0.097
-
2-hydroxypyrimidine apparent Km-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
1.2.3.1 0.173
-
2-hydroxypyrimidine apparent Km-value of native mAOX3, pH 7.4, 25°C Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.3.1 150000
-
SDS-PAGE, native and recombinant protein, degradation products of 130000, 80000, 70000, and 55000 Da in case of purified recombinant mAOX3 Mus musculus
1.2.3.1 300000
-
gel filtration, native and recombinant mAOX3 Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
1.2.3.1 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.3.1 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

EC Number Source Tissue Comment Organism Textmining
1.2.3.1 liver
-
Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.3.1 2-hydroxypyrimidine + H2O + ferricyanide + O2
-
Mus musculus ?
-
?
1.2.3.1 benzaldehyde + 2 ferricyanide + H2O
-
Mus musculus benzoate + 2 ferrocyanide + 2 H+
-
?
1.2.3.1 butanal + 2 ferricyanide + H2O
-
Mus musculus butanoate + 2 ferrocyanide + 2 H+
-
?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.2.3.1 mAOX3
-
Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.3.1 0.733
-
benzaldehyde apparent Kcat-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
1.2.3.1 2.167
-
benzaldehyde apparent Kcat-value of native mAOX3, pH 7.4, 25°C Mus musculus
1.2.3.1 2.333
-
Butanal apparent Kcat-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
1.2.3.1 6.4
-
Butanal apparent Kcat-value of native mAOX3, pH 7.4, 25°C Mus musculus
1.2.3.1 6.88
-
2-hydroxypyrimidine apparent Kcat-value of recombinant mAOX3, pH 7.4, 25°C Mus musculus
1.2.3.1 21.32
-
2-hydroxypyrimidine apparent Kcat-value of native mAOX3, pH 7.4, 25°C Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.3.1 FAD
-
Mus musculus
1.2.3.1 molybdenum cofactor i.e. MoCo Mus musculus
1.2.3.1 [2Fe-2S]-center two distinct ones Mus musculus

General Information

EC Number General Information Comment Organism
1.2.3.1 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