Protein Variants | Comment | Organism |
---|---|---|
additional information | glucose oxidase is chemically modified to increase the stability of GOx using N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride and sodium benzoate or aniline. The modification forms an amide bond between benzoate and lysines or aniline with glutamate and aspartate residues. The labeling of primary amines (lysines and the N-terminus) by benzoate is measured through a trinitrobenzene sulfonic acid (TNBS) assay | Aspergillus niger |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
17.5 | - |
beta-D-glucose | pH 5.1, 37°C, unmodified enzyme | Aspergillus niger | |
23.2 | - |
beta-D-glucose | pH 5.1, 37°C, aniline-modified enzyme | Aspergillus niger | |
32.4 | - |
beta-D-glucose | pH 5.1, 37°C, benzoate-modified enzyme | 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 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
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 |
More | type X-S enzyme | Aspergillus niger |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | 37 | assay at | Aspergillus niger |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification, method development, evaluation, and kinetics of thermal inactivation, detailed overview. Determination of the effect of temperature on the rate constant of inactivation of GOx at each of the selected pressures, and of the pressure effects on the rate constant of inactivation of GOx | Aspergillus niger |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
434 | - |
beta-D-glucose | pH 5.1, 37°C, benzoate-modified enzyme | Aspergillus niger | |
446 | - |
beta-D-glucose | pH 5.1, 37°C, unmodified enzyme and aniline-modified enzyme | Aspergillus niger |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.1 | - |
assay at | Aspergillus niger |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Aspergillus niger |