EC Number   |
|---|
  1.5.1.54 | modeling of the methyltetrahydrofolate product into the enzyme active site and shows 150fold decreased activity |
| 1.5.1.54 | molecular docking of genistein. Gensitein may interfere with the binding site of NADH |
| 1.5.1.54 | structure provides a model for the catalytic domain shared by all MTHFRs. This domain is a beta8alpha8 barrel that binds FAD in a special fashion. Ala 177, corresponding to Ala 222 in human MTHFR, is near the bottom of the barrel and distant from the FAD. The mutation A177V does not affect Km or kcat but instead increases the propensity for bacterial MTHFR to lose its essential flavin cofactor |
| 1.5.1.54 | structures of ligand-free mutants F223L and F223L/E28Q in complex with 5,10-methylentetrahydrofolate, at 1.65 and 1.70 A resolution, respectively. The folate is bound in a catalytically competent conformation, and residue Leu223 undergoes a conformational change similar to that observed for Phe223 in the E28Q-5,10-methylentetrahydrofolate structure |
| 1.5.1.54 | structures of the enzyme complexes of wild-type with NADH and mutant E28Q with methytetrahydrofolate. Residue Gln183 makes key hydrogen-bonding interactions with both NADH and folate in their respective halfreactions |
