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Literature summary for 1.1.3.4 extracted from
- Glucose oxidase from Penicillium amagasakiense characterization of the transition state of its denaturation from molecular dynamics simulations (2014), Proteins, 82, 2353-2363 .
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-D-glucose + O2 | Penicillium amagasakiense | - |
D-glucono-1,5-lactone + H2O2 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Penicillium amagasakiense | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the enzyme has four N-glycosylation sites at positions ASN93, ASN165, ASN357, and ASN392, respectively. Three different sugars are bound at these positions: N-acetyl-D-glucosamine, beta-D-mannose, and alpha-D-mannose | Penicillium amagasakiense |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-D-glucose + O2 | - |
Penicillium amagasakiense | D-glucono-1,5-lactone + H2O2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 66700, alpha/beta-fold, SDS-PAGE | Penicillium amagasakiense |
| More | the monomers of GOx-pa contain 587 amino acids each, and one prosthetic group, flavin adenine dinucleotide (FAD). Dimer interface analysis | Penicillium amagasakiense |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GOX | - |
Penicillium amagasakiense |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
enzyme denaturing process at different temperatures, localization of breaking points, analysis by molecular dynamics simulations, overview. Identification of the transition state of protein folding/unfolding, overview | Penicillium amagasakiense |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Penicillium amagasakiense | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | enzyme denaturing process analysis by molecular dynamics simulations, overview | Penicillium amagasakiense |
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