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1.1.3.4: glucose oxidase

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

Word Map on EC 1.1.3.4

Reaction

beta-D-glucose
+
O2
=
D-glucono-1,5-lactone
+
H2O2

Synonyms

AldO, beta-D-glucose oxidase, beta-D-glucose oxygen-1-oxidoreductase, beta-D-glucose/oxygen 1-oxidoreductase, beta-D-glucose: oxygen 1-oxidoreductase, beta-D-glucose:O2 1-oxidoreductase, beta-D-glucose:O2-1-oxidoreductase, beta-D-glucose:oxygen 1-oxido-reductase, beta-D-glucose:oxygen 1-oxidoreductase, beta-D-glucose:oxygen oxidoreductase, beta-D-glucose:oxygen-1-oxidoreductase, beta-D-glucose:quinone oxidoreductase, CngoxA, corylophyline, D-glucose oxidase, D-glucose-1-oxidase, deoxin-1, glucose aerodehydrogenase, glucose oxyhydrase, glucose-1-oxidase, GO-2, GOD, GOX, GOxP5, microcid, More, notatin, oxidase, glucose, pen-GOx, penatin, yGOXpenag

ECTree

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

Crystallization

Crystallization on EC 1.1.3.4 - glucose oxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of the partially deglycosylated enzyme, crystal structure determined by isomorphous replacement and refined to 2.3 A resolution
-
structure refined at 1.9 A resolution to an R value of 19.0%
tertiary structure determined by x-ray crystallography
vapor diffusion sitting drop method
crystal structure analysis, PDB ID 1GPE
deglycosylation and purification to isoelectric homogeneity are important prerequisite steps to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme are reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 A, b = 136.3 A and c = 156.7 A. Crystallized as a complex with the coenzyme FAD
the enzyme crystallizes from 1.3 M ammonium sulfate, 100 mM citrate/phosphate buffer pH 7.4 in the orthorhombic space group P212121, with unit-cell dimensions a = 57.6, b = 132.1, c = 151.3 A and one dimeric molecule per asymmetric unit. The structure is determined by molecular replacement and refined at 1.8 A resolution to an R value of 16.4%
native wild-type enzyme, hanging-drop vapor diffusion method at 4 °C by mixing equal volumes of 14 mg/mL AldO solution in 50 mM potassium phosphate buffer, pH 7.5, with reservoir solutions containing 0.1 M MES/HCl, pH 6.5, 0.2 M MgCl2 and 18-20% w/v PEG4000, 3-4 days, substrate incorporation by soaking the wild-type AldO crystals in a solution consisting of 0.1 M MES/HCl, pH 6.5, 0.2 M MgCl2, 25% w/v PEG 4000, 17.5% sucrose, and 25 mM substrate for 3 h, X-ray diffraction structure determination and analysis at 1.1-1.9 A resolution
-