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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

pH Stability

pH Stability on EC 1.1.3.4 - glucose oxidase

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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.9
-
stable for 1 h, when FAD is added, bound to Blue Dextran
389798
11
-
at 4°C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
389832
12
-
at 4°C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
389832
2
-
acid-induced unfolding of both forms of enzyme, significant loss of FAD cofactor and secondary structure
654358
2 - 6
stable, recombinant enzyme
763078
2.5
-
the BTL wild-type strain enzyme is slightly more stable than the commercially available enzyme
389831
3 - 11
-
10% relative activity after 30 min at pH 3.0, 40% relative activity after 30 min at pH 4.0, 50% relative activity after 30 min at pH 5.0, 55% relative activity after 30 min at pH 6.0, 100% activity after 30 min at pH 7.0, 95% relative activity after 30 min at pH 8.0, 75% relative activity after 30 min at pH 9.0, 70% relative activity after 30 min at pH 10.0, 55% relative activity after 30 min at pH 11.0
710858
3 - 12
1 h, stable, mutant enzyme Y169C/A211C
763051
3 - 5
-
deglycosylated enzyme, 4°C, 4 months, 65-75% activity retained
389816
3 - 9
3.5 - 7.5
-
-
389792
4 - 5.5
-
-
389795
4 - 9
purified recombinant enzyme, more than 80% of activity is retained after incubation for 1 h at pHs from 4.0 to 9.0 and the maximum activity remains at pH 5.0-8.0
743193
4.5 - 5.2
-
recombinant enzyme, exhibits more than 80% of the maximum activity
389835
4.5 - 6
-
the enzyme shows a pH-dependent response to the high pressure homogenization treatment, with reduction or maintenance of activity at pH 4.5-6.0 and a remarkable activity increase (30-300%) at pH 6.5 at all tested temperatures. i.e. 15°C, 50°C and 75°C
743644
4.5 - 7.4
-
the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx has a higher catalytic activity at pH 7.4, close to the physiological environment, in comparison with that at pH 4.5
699922
4.5 - 9
-
stable
671400
5 - 7
5 - 8
6 - 8
-
-
389789
6 - 9
1 h, stable, recombinant enzyme
763051
6.2 - 6.5
-
recombinant enzyme, exhibits more than 80% of the maximum activity
389835
7.5
-
50% activity
389833
additional information