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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

Purification

Purification on EC 1.2.3.1 - aldehyde oxidase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1667fold by gel filtration with a yield of 12%, to more than 98% purity
231fold purified at a yield of about 1% by heat treatment, ammonium sulfate fractionation, column chromatographies, and hydroxyapatite
55°C, ammonium sulfate, Benzmidine-Sepharose, Mono Q
-
55°C, ammonium sulfate, Mono Q
-
ammonium sulfate precipitation
-
by Ni-NTA column chromatography
heat treatment, Butyl-toyopearl, Resource Q
-
mAOX3 purified from CD1 mouse liver as well as from a heterologous expression system from Escherichia coli, recombinant mAOX3 expressed as an N-terminal fusion protein with a His6 tag
Ni affinity column chromatography
Ni Sepharose 6 Fast Flow column chromatography, HiTrap QHP column chromatography, and HisTrap FF column chromatography
-
partial purification
-
partial purification by heat treatment and ammonium sulfate precipitation
-
partially purified
-
partially purified by heat treatment and ammonium sulfate precipitation
recombinant enzyme, simplified two-step purification method using Ni-NTA and size-exclusion chromatography
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
-
recombinant protein
simultaneous purification with xanthine oxidase
-
to homogeneity, chromatography techniques