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Literature summary for 1.1.3.15 extracted from
- Structures of glycolate oxidase from Nicotiana benthamiana reveal a conserved pH sensor affecting the binding of FMN (2018), Biochem. Biophys. Res. Commun., 503, 3050-3056 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Nicotiana benthamiana |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| apo-GOX structure and its complex structure with cofactor FMN. The binding of FMN induces a pronounced conformational change of the GOX tetramer. A conserved pH sensor found among different species might directly regulate the binding of FMN and the enzyme activity | Nicotiana benthamiana |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 160000 | - |
small-angle X-ray scattering, gel filtration and structural analysis | Nicotiana benthamiana |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Nicotiana benthamiana | E1AXT8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant protein | Nicotiana benthamiana |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 4 * 42000, SDS-PAGE | Nicotiana benthamiana |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FMN | - |
Nicotiana benthamiana |  |
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Release 2023.1 (January 2023)
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