EC Number | Application | Comment | Organism |
---|---|---|---|
1.1.3.4 | analysis | the enzyme is useful as biosensor for glucose detection | Aspergillus niger |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.3.4 | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.3.4 | additional information | - |
additional information | Michaelis-Menten kinetics | Aspergillus niger | |
1.1.3.4 | 0.019 | - |
beta-D-glucose | native enzyme in solution, pH 5.5, temperature not specified in the publication | Aspergillus niger | |
1.1.3.4 | 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 | |
1.1.3.4 | 12 | - |
beta-D-glucose | enzyme adsorbed on 11-amino-1-undecanethiol coated matrix, pH 5.5, temperature not specified in the publication | Aspergillus niger | |
1.1.3.4 | 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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.1.3.4 | soluble | - |
Aspergillus niger | - |
- |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.4 | beta-D-glucose + O2 | Aspergillus niger | - |
D-glucono-1,5-lactone + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.3.4 | Aspergillus niger | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.1.3.4 | commercial preparation | - |
Aspergillus niger | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.1.3.4 | 100 | - |
immobilized enzyme, pH 5.5, temperature not specified in the publication, high enzyme concentration | Aspergillus niger |
1.1.3.4 | 216 | - |
immobilized enzyme, pH 5.5, temperature not specified in the publication, low enzyme concentration | Aspergillus niger |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.4 | beta-D-glucose + O2 | - |
Aspergillus niger | D-glucono-1,5-lactone + H2O2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.3.4 | GOX | - |
Aspergillus niger |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.3.4 | 5.5 | - |
assay at | Aspergillus niger |