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Literature summary for 5.3.1.5 extracted from
- Arthrobacter D-xylose isomerase: chemical modification of carboxy groups and protein engineering of pH optimum (1993), Biochem. J., 296, 685-691.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D189L | the Glu140Lys and Asp189Lys mutant proteins are synthesized in the Escherichia coli host, but are incapable of folding correctly. Mutant Trp136Glu does not show any enzyme activity | Arthrobacter sp. |
| E140L | the Glu140Lys and Asp189Lys mutant proteins are synthesized in the Escherichia coli host, but are incapable of folding correctly. Mutant Trp136Glu does not show any enzyme activity | Arthrobacter sp. |
General Stability
| General Stability | Organism |
|---|---|
| glycinamidylated enzyme is less stable than the native enzyme in 8 M urea or on heating | Arthrobacter sp. |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arthrobacter sp. | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Arthrobacter sp. |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-Xylose | - |
Arthrobacter sp. | D-Xylulose | - |
? |  |
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