1.1.3.9: galactose oxidase

This is an abbreviated version!
For detailed information about galactose oxidase, go to the full flat file.

Word Map on EC 1.1.3.9

Reaction

D-galactose
+
O2
=
D-galacto-hexodialdose
+
H2O2

Synonyms

AOd, beta-galactose oxidase, D-galactose oxidase, FgrGalOx, galactose 6-oxidase, galactose oxidase, GalOx, GAO, GAOA, GAOX, GO, GOase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.9 galactose oxidase

Crystallization

Crystallization on EC 1.1.3.9 - galactose oxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of W290F and W290G are grown from protein as isolated, using hanging drop vapor diffusion from 1 to 2 M (NH4)2SO4 and 0.1 M sodium acetate at pH 4.0-5.0. To prepare the azide complex, wild-type galactose oxidase is dialyzed into 50 mM PIPES (pH 7.0) for 2 h, before addition of 20 mM sodium iethyl dithiocarbamate (DDC). The copper chelator DDC promotes the formation of orthorhombic crystals, which have more favorable crystal packing for substrate soaking experiments. The copper-free protein is crystallized in 13.5% PEG 8000, 200 mM calcium acetate, and 100 mM MES (pH 6.3)
sitting drop method. 2-5 mg/ml of enzyme mixed with equal volume of well solution. Crystals are soaked in oxygen-free Cu2+ solutions
wild-type enzyme and W290F mutant enzyme crystal structure analysis, PDB IDs 2EIE and 2EIC, respectively
mutant C383S
-
ammonium sulfate precipitation, 1.7 A resolution
-
analysis of crystal structure, PDB ID 1GOF, of the processed (cofactor formed) Cu(II) site reveals the active site ligation. Residues His496, His581, cysteinylated-Tyr272, and an acetate ion form the four equatorial ligands. In the structure of Cu(II)-GO crystallized without acetate, PDB ID 1GOG, the fourth equatorial position is occupied by a weakly bound water. A second tyrosine, Tyr495, occupies an axial position with a Cu-O 2.6–2.7 A distance in these structures. Spectroscopical characterization of the geometric structure of the pre-processed Cu(I) active site using Cu K-edge X-ray absorption spectroscopy. Molecular modeling of the pre-processed Cu(I)-galactose oxidase active site and biogenesis reaction coordinate
-
hanging drop vapor diffusion, 1.7 A resolution
-
sitting drop vapour diffusion, native, recombinant and mutant enzymes
-