Application | Comment | Organism |
---|---|---|
diagnostics | the enzyme is used as a molecular diagnostic and analytical tool in the medical industry for the control of diabetes | Aspergillus niger |
food industry | the enzyme is used as food preservative and color stabilizer | Aspergillus niger |
synthesis | the enzyme is used in the production of gluconic acid | Aspergillus niger |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Aspergillus niger | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
160000 | - |
- |
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 | P13006 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | most of the carbohydrate moieties contain mannose | Aspergillus niger |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-D-glucose + O2 | - |
Aspergillus niger | D-glucono-1,5-lactone + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 80000, SDS-PAGE | Aspergillus niger |
Synonyms | Comment | Organism |
---|---|---|
GOD | - |
Aspergillus niger |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
assay at | Aspergillus niger |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
analysis of thermal inactivation kinetics of enzyme GOD | Aspergillus niger |
55 | - |
purified dimeric enzyme, pH 5.8, stable up to, rapid inactivation above, the enzyme forms aggregates at incubation temperatures above 55°C, overview | Aspergillus niger |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.8 | - |
assay at | Aspergillus niger |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | each monomer has one co-enzyme molecule of FAD, which acts as an electron receptor during catalysis | Aspergillus niger |