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Literature summary for 2.1.1.45 extracted from
- Substrate channeling between the human dihydrofolate reductase and thymidylate synthase (2016), Protein Sci., 25, 79-86 .
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydrofolate + dUMP | Homo sapiens | - |
dihydrofolate + dTMP | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P04818 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydrofolate + dUMP | - |
Homo sapiens | dihydrofolate + dTMP | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | in vitro, one human thymidylate synthase dimer binds to up to six human dihydrofolate reductase monomers, protein-protein docking process, overview. Existence of bound-state conformations of the human DHFR and TS proteins where a continuous positive surface potential region, connecting the TS and DHFR active sites, is formed | Homo sapiens |
| physiological function | the human thymidylate synthase and dihydrofolate reductase catalyse two consecutive reactions in the folate metabolism pathway and are very likely to bind in the same multi-enzyme complex in vivo, substrate channeling occurs between the human thymidylate synthase and dihydrofolate reductase, analysis by protein-protein docking, electrostatics calculations, and Brownian dynamics, overview. The non-covalently bound human thymidylate synthase and dihydrofolate reductase are capable of substrate channeling and the formation of the surface electrostatic highway. The substrate channeling efficiency between the two can be reasonably high and comparable to that of the bifunctional protozoan enzyme | Homo sapiens |
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