Application | Comment | Organism |
---|---|---|
analysis | the enzyme is useful as biosensor for glucose detection | Aspergillus niger |
Protein Variants | Comment | Organism |
---|---|---|
A449C | site-directed mutagenesis, the mutation results in almost completely diminished activity compared to the wild-type enzyme | Aspergillus niger |
E84C | site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity | Aspergillus niger |
H447C | site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity | Aspergillus niger |
additional information | engineering of glucose oxidase by site-specific attachment of a maleimide-modified gold nanoparticle to the enzyme for enabling direct electrical communication between the conjugated enzyme and an electrode required for using the enzyme as biosensor, evaluation, overview | Aspergillus niger |
S307C | site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity | Aspergillus niger |
T56V/T132S | site-directed mutagenesis, the mutant shows improved catalytic efficiency. The protein has three native cysteines, of which two are involved in a disulfide bond and the third is a free cysteine, Cys 521 | Aspergillus niger |
T56V/T132S/C521S | site-directed mutagenesis, the mutant shows improved catalytic efficiency, mutation C521S does not alter enzyme activity, but the attachment of AuNPs to the native free thiol is prevented | Aspergillus niger |
Y435C | site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity | Aspergillus niger |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics, overview | Aspergillus niger | |
6.3 | - |
beta-D-glucose | wild-type enzyme conjugated to gold nanoparticles, pH and temperature not specified in the publication | Aspergillus niger | |
8.2 | - |
beta-D-glucose | mutant H447C conjugated to gold nanoparticles, pH and temperature not specified in the publication | Aspergillus niger | |
15 | - |
beta-D-glucose | mutant H447C, pH and temperature not specified in the publication | Aspergillus niger | |
96.4 | - |
beta-D-glucose | wild-type enzyme, pH and temperature not specified in the publication | Aspergillus niger |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-D-glucose + O2 | Aspergillus niger | GOx enzyme catalyzes the oxidation of glucose to gluconolactone via reduction of the FAD cofactor to FADH2. The reoxidation of FADH2 in the ping-pong mechanism is normally achieved using oxygen as the electron acceptor | D-glucono-1,5-lactone + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus niger | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-D-glucose + O2 | GOx enzyme catalyzes the oxidation of glucose to gluconolactone via reduction of the FAD cofactor to FADH2. The reoxidation of FADH2 in the ping-pong mechanism is normally achieved using oxygen as the electron acceptor | Aspergillus niger | D-glucono-1,5-lactone + H2O2 | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
22.8 | - |
beta-D-glucose | wild-type enzyme conjugated to gold nanoparticles, pH and temperature not specified in the publication | Aspergillus niger | |
55.3 | - |
beta-D-glucose | mutant H447C conjugated to gold nanoparticles, pH and temperature not specified in the publication | Aspergillus niger | |
152 | - |
beta-D-glucose | wild-type enzyme, pH and temperature not specified in the publication | Aspergillus niger | |
425 | - |
beta-D-glucose | mutant H447C, pH and temperature not specified in the publication | Aspergillus niger |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Aspergillus niger |