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Literature summary for 1.1.3.4 extracted from
- Production and characterization of recombinant glucose oxidase from Aspergillus niger expressed in Pichia pastoris (2014), Lett. Appl. Microbiol., 58, 393-400 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene gox, recombinant expression of the extracellular enzyme in Pichia pastoris strain GS115 | Aspergillus niger |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2,4-dichlorphenoxyacetic acid | decreases the enzyme activity by about 70% at 2 mM | Aspergillus niger |  |
| Ag+ | complete inhibition at 2 mM | Aspergillus niger | |
| Cu2+ | complete inhibition at 2 mM | Aspergillus niger | |
| DTNB | complete inhibition at 2 mM | Aspergillus niger | |
| DTT | complete inhibition at 2 mM | Aspergillus niger | |
| Fe2+ | complete inhibition at 2 mM | Aspergillus niger | |
| Hg2+ | 93% inhibition at 2 mM | Aspergillus niger | |
| lecithin | 6% inhibition at 2% | Aspergillus niger | |
| additional information | diethyl dicarbonate, dimethylaminobenzaldehyde, and EDTA do not cause any inhibition at 2 mM. SDS, Tween-20, Tween-80, Triton X-100, NP40, benzalkonium bromide, and sodium cholate do not exhibit a significant effect on the enzyme activity at 2% | Aspergillus niger | |
| NaF | decreases the enzyme activity by about 5% at 2 mM | Aspergillus niger | |
| NaN3 | decreases the enzyme activity by about 8% at 2 mM | Aspergillus niger | |
| PMSF | decreases the enzyme activity by about 18% at 2 mM | Aspergillus niger | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Aspergillus niger | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the enzyme activity is not significantly affected by 2 mM of Mg2+, Ca2+, Mn2+, Ni2+, Al3+, and Zn2+ | Aspergillus niger |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 150000 | - |
- |
Aspergillus niger |
Natural Substrates/ Products (Substrates)
| 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 | - |
? | |
| beta-D-glucose + O2 | Aspergillus niger ATCC 9029 | - |
D-glucono-1,5-lactone + H2O2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | Q0PGS3 | - |
- |
| Aspergillus niger ATCC 9029 | Q0PGS3 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | - |
Aspergillus niger |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant extracellular enzyme 1.26fold from Pichia pastoris by anion exchange chromatography | Aspergillus niger |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 155 | - |
purified recombinant enzyme, pH 6.0, 40°C | Aspergillus niger |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-D-glucose + O2 | - |
Aspergillus niger | D-glucono-1,5-lactone + H2O2 | - |
? | |
| beta-D-glucose + O2 | - |
Aspergillus niger ATCC 9029 | D-glucono-1,5-lactone + H2O2 | - |
? | |
| additional information | the enzyme is specific for D-glucose, it shows less than 10% activity with trehalose, D-galactose, melibiose, and raffinose compared to D-glucose, no activity with L-mannomethylose, D-fructose, D-xylose, lactose, and sucrose | Aspergillus niger | ? | - |
? | |
| additional information | the enzyme is specific for D-glucose, it shows less than 10% activity with trehalose, D-galactose, melibiose, and raffinose compared to D-glucose, no activity with L-mannomethylose, D-fructose, D-xylose, lactose, and sucrose | Aspergillus niger ATCC 9029 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 75000, recombinant enzyme, SDS-PAGE | Aspergillus niger |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GOX | - |
Aspergillus niger |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
recombinant enzyme | Aspergillus niger |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 60 | the activity gradually increases from 25°C to 40°C, but followed by a decrease at higher temperatures | Aspergillus niger |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 60 | purified recombinant enzyme, more than 90% activity remaining after incubation for 30 min at 50°C and 54% at temperatures up to 55°C | Aspergillus niger |
| 50 | - |
the purified recombinant enzyme retains 90% activity at 50°C for 30 min | Aspergillus niger |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
recombinant enzyme | Aspergillus niger |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 9 | purified recombinant enzyme, more than 80% of activity is retained after incubation for 1 h at pHs from 4.0 to 9.0 and the maximum activity remains at pH 5.0-8.0 | Aspergillus niger |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Aspergillus niger | |
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