Application | Comment | Organism |
---|---|---|
analysis | the enzyme is useful as biosensor for glucose detection | Aspergillus niger |
Protein Variants | Comment | Organism |
---|---|---|
additional information | enzyme adsorption on different particles with homogeneous or nanostructured surfaces and coated with different compounds, i.e. 11-amino-1-undecanethiol, 12-mercaptododecanoic acid, 1-dodecanethiol, and 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol), only 9% of the activity of the native protein is preserved on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol), but the substrate affinity of the adsorbed GOx is best on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) where its catalytic activity is worst, secondary structure of thhe enzyme is altered compared to enzyme in solution, overview | Aspergillus niger |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Aspergillus niger | |
0.019 | - |
beta-D-glucose | native enzyme in solution, pH 5.5, temperature not specified in the publication | Aspergillus niger | |
8 | - |
beta-D-glucose | enzyme adsorbed on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) coated matrix, high enzyme concentration, pH 5.5, temperature not specified in the publication | Aspergillus niger | |
12 | - |
beta-D-glucose | enzyme adsorbed on 11-amino-1-undecanethiol coated matrix, pH 5.5, temperature not specified in the publication | Aspergillus niger | |
22 | - |
beta-D-glucose | enzyme adsorbed on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) coated matrix, low enzyme concentration, pH 5.5, temperature not specified in the publication | Aspergillus niger |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
soluble | - |
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 | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Aspergillus niger | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
100 | - |
immobilized enzyme, pH 5.5, temperature not specified in the publication, high enzyme concentration | Aspergillus niger |
216 | - |
immobilized enzyme, pH 5.5, temperature not specified in the publication, low enzyme concentration | Aspergillus niger |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-D-glucose + O2 | - |
Aspergillus niger | D-glucono-1,5-lactone + H2O2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GOX | - |
Aspergillus niger |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
assay at | Aspergillus niger |