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Literature summary for 2.4.2.4 extracted from
- Stabilization of thymidine phosphorylase from Escherichia coli by immobilization and post immobilization techniques (2011), Enzyme Microb. Technol., 49, 52-58.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | immobilization of enzyme on solid support with the aim to have a stable and recyclable biocatalyst for nucleoside synthesis. Immobilization by ionic adsorption on amine-functionalized agarose and Sepabeads results in more than 85% activity recovery. Cross-linking with aldehyde dextran, MW20 kDa, decreases the percentage of expressed activity after immobilization by about 25%, but results in up to 6fold and 3fold higher stability than the soluble enzyme and the non-cross-linked counterpart, respectively, at pH 10 and 37°C. The preparation can be successfully used for the one-pot synthesis of 5-fluoro-2'-deoxyuridine starting from 2'-deoxyuridine or thymidine and 5-fluorouracil. In both cases, the reaction proceeds at the same rate leading to 62% conversion in 1 h | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Escherichia coli | - |
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Release 2023.1 (January 2023)
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