Application | Comment | Organism |
---|---|---|
additional information | despite the broad range of applications for glucose oxidase, the effectiveness of glucose oxidase is restricted by the narrow substrate range of this enzyme and susceptibility to H2O2 inactivation | Aspergillus niger |
Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged enzyme in Pichia pastoris strain KM71H | Aspergillus niger |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
H2O2 | loss of 40% activity on D-glucose at 200 mM H2O2 | Aspergillus niger |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-D-glucose + O2 | Aspergillus niger | - |
D-glucono-1,5-lactone + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus niger | Q9HFQ1 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-D-glucose + O2 | - |
Aspergillus niger | D-glucono-1,5-lactone + H2O2 | - |
? | |
beta-D-glucose + O2 | the enzyme is highly specific for D-glucose | Aspergillus niger | D-glucono-1,5-lactone + H2O2 | - |
? | |
additional information | the enzyme oxidizes the anomeric carbon of beta-D-glucose using molecular oxygen as an electron acceptor, producing H2O2 and D-glucono-delta-lactone, which in the presence of water spontaneously hydrolyzes to gluconic acid. Poor activity with xylose, maltose, cellobiose, cellotetraose, and xylo-oligosaccharides | Aspergillus niger | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Aspergillus niger |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
assay at | Aspergillus niger |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | a flavoenzyme with a tightly but non-covalently bound FAD cofactor | Aspergillus niger |
General Information | Comment | Organism |
---|---|---|
evolution | glucose oxidase (GO) belongs to the auxiliary activity family AA3_2 | Aspergillus niger |
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 | Aspergillus niger |
additional information | narrow binding pocket of glucose oxidase | Aspergillus niger |