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Literature summary for 2.1.1.45 extracted from
- Complete restoration of activity to inactive mutants of Escherichia coli thymidylate synthase: Evidence that E. coli thymidylate synthase is a half-the-sites activity enzyme (1995), Biochemistry, 34, 1469-1474.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Escherichia coli |
- |
Lacticaseibacillus casei |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydrofolate + dUMP | Escherichia coli | - |
dihydrofolate + dTMP | - |
? |  |
| 5,10-methylenetetrahydrofolate + dUMP | Lacticaseibacillus casei | - |
dihydrofolate + dTMP | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Lacticaseibacillus casei | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydrofolate + dUMP | - |
Escherichia coli | dihydrofolate + dTMP | - |
? | |
| 5,10-methylenetetrahydrofolate + dUMP | - |
Escherichia coli | dihydrofolate + dTMP | - |
r | |
| 5,10-methylenetetrahydrofolate + dUMP | - |
Lacticaseibacillus casei | dihydrofolate + dTMP | - |
? | |
| 5,10-methylenetetrahydrofolate + dUMP | - |
Lacticaseibacillus casei | dihydrofolate + dTMP | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Escherichia coli |
| dimer | - |
Lacticaseibacillus casei |
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