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Literature summary for 2.4.2.4 extracted from
- Computational studies of the domain movement and the catalytic mechanism of thymidine phosphorylase (1999), Proteins, 37, 242-252.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate | mechanism | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| thymidine + phosphate | - |
Escherichia coli | thymine + 2-deoxy-D-ribose 1-phosphate | - |
r |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | dual substrate enzyme with two domains | Escherichia coli |
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Release 2023.1 (January 2023)
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