Inhibitors | Comment | Organism | Structure |
---|---|---|---|
5F-dUMP | mechanism-based inhibitor | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5,10-methylenetetrahydrofolate + dUMP | - |
Escherichia coli | dihydrofolate + dTMP | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | the nucleotide binds to the free and singly bound forms of the enzyme with nearly equal affinity over a broad range of temperatures and in multiple buffers. There are small but significant differences in DELTACP for the two binding event, so the active sites are not formally equivalent. There is little-to-no allostery at the level of DELTAGbind. There is minor inter-subunit cooperativity in formation of a ternary complex with the mechanism-based inhibitor, 5F-dUMP, and cofactor | Escherichia coli |