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Literature summary extracted from
- Kinetic characterization of bifunctional thymidylate synthase-dihydrofolate reductase (TS-DHFR) from Cryptosporidium hominis: a paradigm shift for ts activity and channeling behavior (2004), J. Biol. Chem., 279, 18314-18322.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.5.1.3 | Cryptosporidium hominis | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.1.3 | 7,8-dihydrofolate + NADPH | clear evidence against dihydrofolate substrate channeling in the bifunctional thymidylate synthase-dihydrofolate reductase | Cryptosporidium hominis | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.5.1.3 | thymidylate synthase-dihydrofolate reductase | bifunctional enzyme | Cryptosporidium hominis |
| 1.5.1.3 | TS-DHFR | bifunctional enzyme | Cryptosporidium hominis |
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Release 2023.1 (January 2023)
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