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Literature summary for 6.3.2.17 extracted from
- Docking studies and ligand recognition in folylpolyglutamate synthetase (2005), J. Med. Chem., 48, 7764-7772.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lacticaseibacillus casei | P15925 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | there are two possible sites for binding folate substrates. The di- and triglutamate substrates can be accommodated in both sites in a way appropriate for the ligation reaction, but only the new pocket appears to bind mTHF and allow the initial ligation reaction. It is suggested that the new pocket plays an essential role in the first turnover to create folylpoly-glutamates | Lacticaseibacillus casei | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FPGS | - |
Lacticaseibacillus casei |
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Release 2023.1 (January 2023)
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