1.5.1.54: methylenetetrahydrofolate reductase (NADH)
This is an abbreviated version!
For detailed information about methylenetetrahydrofolate reductase (NADH), go to the full flat file.
Reaction
Synonyms
5,10-CH2-H4folate reductase, 5,10-methylenetetrahydrofolate reductase, 5,10-methylenetetrahydrofolate reductase (FADH2), 5,10-methylenetetrahydrofolic acid reductase, 5,10-methylenetetrahydropteroylglutamate reductase, 5-methyltetrahydrofolate:(acceptor) oxidoreductase, metF, methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase, methylenetetrahydrofolate reductase, methylenetetrahydrofolic acid reductase, MSMEG_6596, MSMEG_6649, MTHFR1, MTHFR2, N5,10-methylenetetrahydrofolate reductase, N5,N10-methylenetetrahydrofolate reductase
ECTree
1.5.1.54 methylenetetrahydrofolate reductase (NADH)Advanced search results
results (
results (Crystallization
Crystallization on EC 1.5.1.54 - methylenetetrahydrofolate reductase (NADH)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
modeling of the methyltetrahydrofolate product into the enzyme active site and shows 150fold decreased activity
molecular docking of genistein. Gensitein may interfere with the binding site of NADH
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
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
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
