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1.17.3.2: xanthine oxidase

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

Word Map on EC 1.17.3.2

Reaction

xanthine
+
H2O
 +
O2
=
Urate
 +
H2O2

Synonyms

AXOR, EC 1.1.3.22, EC 1.2.3.2, EC 1.2.3.2., hypoxanthine oxidase, hypoxanthine-xanthine oxidase, hypoxanthine:oxygen oxidoreductase, More, oxidase, xanthine, Schardinger enzyme, xanthine dehydrogenase/oxidase, xanthine oxidase, xanthine oxidoreductase, xanthine: oxygen oxidoreductase, xanthine:O2 oxidoreductase, xanthine:oxygen oxidoreductase, xanthine:xanthine oxidase, XnOx, XO, XOD, XOR

ECTree

     1 Oxidoreductases
         1.17 Acting on CH or CH2 groups
             1.17.3 With oxygen as acceptor
                1.17.3.2 xanthine oxidase

Crystallization

Crystallization on EC 1.17.3.2 - xanthine oxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.5 A resolution, each enzyme subunit is composed of an N-terminal 20000 Da domain containing two iron sulfur centers, a central 40000 Da FAD domain and a C-terminal 85000 molybdopterin binding domain, the four redox centers are aligned in a linear fashion
-
batch method most suitable for crystallization
-
crystal structure determination and analysis of the enzyme in complex with a variety of substrates and substrate analogues, e.g. with 2-hydroxy-6-methylpurine or hypoxanthine, X-ray diffraction structure analysis at 1.8-3.1 A resolution
-
crystal structures for bovine xanthine oxidase in complex with indole-3-acetaldehyde and guanine, both at 1.6 A resolution is reported. In the case of indole-3-acetaldehyde, a modest, sterically allowed rotation juxtaposes the aldehyde group with the molybdenum center that allows hydroxylation to take place. With guanine, the substrate must rotate approximately 180° to present its 8 position to the active site molybdenum center for hydroxylation, and this rotation is sterically prohibited
-
enzme in complex with inhibitor quercetin, X-ray diffraction structure determintion and analysis at 2.0 A resolution
enzyme in complex with inhibitor 2-hydroxy-6-methylpurine, 10 mg/ml purified enzyme in 40 mM Tris-HCl, pH 7.8, 20 mM diphosphate, pH 8.5, 0.2 mM EDTA and 5 mM DTT, batch method mixing 0.02 ml of protein solution and 0.01 ml of precipitant solution, the latter containing of 12-14% PEG 8000, 0.1 M potassium phosphate, and 0.2 mM EDTA, pH 7.2, for 2-3 days at 25°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
purified enzyme in complex with hypoxanthine or 6-mercaptopurine, mixing of 0.01 ml of 5 mg/ml protein solution with 0.005-0.006 ml of 12% polyethylene glycol 8000 solution, at pH 7.0, crystallization in the darkness at 25°C, ligand binding by soaking of crystals, X-ray diffraction structure determination and analysis at 1.8 and 2.6 A resolution, respectively
urate complexes of the reduced form of native milk enzyme reaction intermediate, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
purified recombinant mutant E308V, 15mg/ml protein in 5 mM Tris, pH 8.5, containing 1mM sodium salicylate and 0.1mM EDTA, incubation with 5 mM dithiothreitol for 1 h at room temperature, aliquots of 0.005 ml protein solution are mixed with 0.005 ml of 100 mM sodium citrate, pH 5.0, containing 8-11% polyethylene glycol 8000, 5 mM DTT, 1 mM sodium salicylate, 0.1 mM EDTA, and placed on siliconized glass plates, 7 days at 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution
-
2.25 A resolution, enzyme contains a molybdoptererin cofactor and two different [2Fe-2S] centers, enzyme is folded into four domains, the first two bind the iron sulfur centers, the last two are involved in molybtopterin binding
Megalodesulfovibrio gigas
-
purified recombinant C-terminally truncated mutant enzyme, crystals of the mutant protein are prepared in two ways: (a) crystallization of the protein directly after DTT treatment and (b) crystallization in the presence of DTT followed by extended soaks in mother liquor devoid of DTT to convert most of the protein to the XO form, X-ray diffraction structure determination and analysis at 2.0 A resolution. Comparisons of crystal structures of a stable wild-type XDH enzyme form, the triple mutant C535A/C992R/C1324, and the DELTAC truncated mutant XOR
W335A/F336L double mutant enzyme crystal structure analysis
-
xanthine oxidoreductase mutant W335A/F336L, showing two similar, but not identical subunits. The cluster involved in conformation-switching is completely disrupted in one subunit, but remains partly associated in the other. Xanthine oxidase and oxidoreductase forms of the mutant are in equilibrium that greatly favors the oxidase form, but upon incubation with dithiothreitol equilibrium is partly shifted towards the oxidoreductase form
XOR complexed with the artificial substrate 4-[5-pyridine-4-yl-1H-[1,2,4]triazol-3-yl]pyridine-2-carbonitril, FYX-051, crystal structure analysis. Urate complexes of the purified recombinant demolybdo-form of mutant D428A, X-ray diffraction structure determination and analysis at 1.7 A resolution