EC Number   |
General Information |
Reference |
|---|
   1.1.3.4 | evolution |
glucose oxidase (GO) belongs to the auxiliary activity family AA3_2 |
743824 |
| 1.1.3.4 | malfunction |
comparison of the substrate profile and H2O2 inactivation of the wild-type glucose oxidase, EC 1.1.3.4, and the Y300A mutant variant of GOOX, the mutant shows a comparatively broad substrate range along with reduced substrate inhibition compared to glucose oxidase, overview |
743824 |
| 1.1.3.4 | malfunction |
enzyme mutant M12 GOx (N2Y/K13E/T30V/I94V/K152R) shows a 3fold higher activity compared to the wild type at 5 mM glucose and two times higher activity at 200 mM glucose |
743277 |
| 1.1.3.4 | more |
424 is a key position for enzyme activity of the immobilized enzyme on electrode surfaces, overview |
742360 |
| 1.1.3.4 | more |
a stable secondary conformation with some degree of freedom at the active sites is essential for the bioelectrocatalytic activity of GOx |
741479 |
| 1.1.3.4 | more |
enzyme denaturing process analysis by molecular dynamics simulations, overview |
743759 |
| 1.1.3.4 | more |
enzyme structure and structure-activity relationship analysis and molecular dynamic simulations, detailed overview. Active-site residues of pen-GOx are two histidines, His520 and His563, which act as general base and general acid in the reductive half-reaction and the oxidative half-reaction, respectively |
743111 |
| 1.1.3.4 | more |
identification and analysis of structural motifs of the protein which are critical for its stability |
-, 743597 |
| 1.1.3.4 | more |
narrow binding pocket of glucose oxidase |
743824 |
| 1.1.3.4 | physiological function |
caterpillar labial salivary enzyme glucose oxidase plays an important role in plant-insect interactions by suppressing the caterpillar-induced nicotine production in tobacco plants |
724133 |
