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Literature summary for 1.1.99.28 extracted from
- Control of the association state of tetrameric glucose-fructose oxidoreductase from Zymomonas mobilis as the rationale for stabilization of the enzyme in biochemical reactors (1998), J. Biochem., 124, 280-286.
General Stability
| General Stability | Organism |
|---|---|
| guanidinium hydrochloride inactivates by induction of structural transitions that are comparable to that observed during substrate turnover. This leads to time-dependent formation of high-order associates and consequently inactivation | Zymomonas mobilis |
| inactivation during substrate turnover. The process of inactivation is triggered by structural transitions that are induced by the lactone product and involves aggregation as the ultimate cause of irreversible inactivation | Zymomonas mobilis |
| urea, 1.0 M, prevents the formation of high-order associates and increases the half-life under operational conditions 10fold | Zymomonas mobilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Zymomonas mobilis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucose + D-fructose | - |
Zymomonas mobilis | D-glucono-1,5-lactone + D-sorbitol | - |
? |  |
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Release 2023.1 (January 2023)
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