EC Number   |
Reaction |
Reference |
|---|
    1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ |
Ala16, Ile51, Cys59, Ser108 and Ile164 are active site residues |
703160 |
| 1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ |
Ala16, Ile51, Cys59, Ser108 and Ile164 are active site residues, catalytic mechanism, overview |
703329 |
| 1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ |
analysis of higher energy conformational substrates by NMR relaxation dispersion. The maximum hydride transfer and steady-state turnover rates are governed by the dynamics of transitions between ground and excited states of the intermediates. Model of conformational changes during the catalytic cycle |
677124 |
| 1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ |
bifunctional proteins with DHFR and thymidylate synthase activity |
392290 |
| 1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ |
binding of NADPH is accompanied by release of 38 water molecules, while binding of dihydrofolate is accompanied by the net uptake of water |
687783 |
| 1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ |
catalytic mechanism |
392207, 392208, 392212 |
| 1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ |
cofactor binding mechanism, pH-dependence investigation |
392212 |
| 1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ |
donor carbon at the hydride transfer transition state resembles the reactant state more than the product state, whereas the acceptor carbon is more productlike, a symptom of transition state imbalance |
674153 |
| 1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ |
in Plasmodium bifunctional thymidylate synthase-dihydrofolate reductase, the overall rate-limiting step is thymidylate synthase catalysis.If thymidylate synthase is in an activated liganded conformation, the dihydrofolate reductase is 2-fold activated. The thymidylate synthase rate is also reciprocally activated by 1.5-fold if dihydrolfolate reductase is in an activated, ligand-bound conformation |
-, 685197 |
| 1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ |
inhibitor binding mechanism |
392210, 392211 |
