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Literature summary for 3.1.1.17 extracted from
- Coimmobilization of gluconolactonase with glucose oxidase for improvement in kinetic property of enzymatically induced volume collapse in ionic gels (2002), Biomacromolecules, 3, 625-631.
Application
| Application | Comment | Organism |
|---|---|---|
| molecular biology | coimmobilization with glucose oxidase in polyelectrolyte gels for improvement of kinetic properties, active enzymes in the gel undergo a shrinking process due to a sudden drop in pH, gel volume phase transition, overview | Aspergillus niger |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 100fold | Aspergillus niger |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| D-glucono-1,5-lactone + H2O = D-gluconate | Acts on a wide range of hexose-1,5-lactones. The hydrolysis of L-gulono-1,5-lactone was previously listed as EC 3.1.1.18, aldonolactonase. | Aspergillus niger |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucono-1,5-lactone + H2O | - |
Aspergillus niger | D-gluconate | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GL | - |
Aspergillus niger |
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Release 2023.1 (January 2023)
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