EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.1.45 | expression in Escherichia coli | Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.1.1.45 | hanging drop method at room temperature, the complexes of mutant TS with dUMP crystallize in the cubic form, binary and ternary complexes with 5NO2dUMP crystallize in the hexagonal form | Escherichia coli |
2.1.1.45 | mutant K48Q, in complex with dUMP or 5-nitro-dUMP, to 2.2 A and 2.7 A resolution, respectively. Binding of dUMP is not impaired in the mutant | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.1.1.45 | K48Q | 430fold decrease in kcat value, about 30fold increase in Km value for (R)-5,10-methylene-5,6,7,8-tetrahydrofolate. Decrease in binding affinity for folate-like inhibitors | Escherichia coli |
2.1.1.45 | K48Q | mutant of Escherichia coli thymidylate synthase | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.45 | (S)-2-(5(((1,2-dihydro-3-methyl-1-oxobenzo(f)quinazolin-9-yl)methyl)amino)1-oxo-2-isoindolinyl)glutaric acid | BW1843U89, U89, distorts the thymidylate synthase active site | Escherichia coli | |
2.1.1.45 | 10-propargyl-5,8-dideazafolate | PDDF, folate-like TS inhibitor | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.1.1.45 | 0.05 | - |
dUMP | 10fold higher than wild-type thymidylate synthase | Escherichia coli | |
2.1.1.45 | 0.05 | - |
dUMP | mutant K48Q | Escherichia coli | |
2.1.1.45 | 0.3 | - |
(R)-5,10-methylene-5,6,7,8-tetrahydrofolate | 30fold higher than wild-type thymidylate synthase | Escherichia coli | |
2.1.1.45 | 0.3 | - |
(R)-5,10-methylenetetrahydrofolate | mutant K48Q | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.45 | 5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP | Escherichia coli | thymidylate synthase is the third enzyme in the methylene tetrahydrofolate cycle besides dihydrofolate reductase and serine hydroxymethyltransferase, in many organisms, thymidylate synthase is the only de novo source for dTMP required for DNA synthesis | 7,8-dihydrofolate + dTMP | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.45 | Escherichia coli | P0A884 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.1.1.45 | after purification and precipitation with ammonium sulfate, wild-type and K48Q TS are frozen at -80°C | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.45 | (R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP | - |
Escherichia coli | 7,8-dihydrofolate + dTMP | - |
? | |
2.1.1.45 | (R)-5,10-methylenetetrahydrofolate + dUMP | - |
Escherichia coli | dihydrofolate + dTMP | - |
? | |
2.1.1.45 | 5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP | - |
Escherichia coli | 7,8-dihydrofolate + dTMP | - |
? | |
2.1.1.45 | 5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP | thymidylate synthase is the third enzyme in the methylene tetrahydrofolate cycle besides dihydrofolate reductase and serine hydroxymethyltransferase, in many organisms, thymidylate synthase is the only de novo source for dTMP required for DNA synthesis | Escherichia coli | 7,8-dihydrofolate + dTMP | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.1.1.45 | 0.016 | - |
dUMP | mutant K48Q | Escherichia coli |