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1.5.1.20: methylenetetrahydrofolate reductase [NAD(P)H]

This is an abbreviated version!
For detailed information about methylenetetrahydrofolate reductase [NAD(P)H], go to the full flat file.

Word Map on EC 1.5.1.20

Reaction

5-methyltetrahydrofolate
+
NAD(P)+
=
5,10-methylenetetrahydrofolate
 +
NAD(P)H
 +
H+

Synonyms

10-methylenetetrahydrofolate reductase, 5,10-CH2-H4folate reductase, 5,10-methylenetetrahydrofolate reductase, 5,10-methylenetetrahydrofolate reductase (FADH2), 5,10-methylenetetrahydrofolate reductase (NADPH), 5,10-methylenetetrahydrofolic acid reductase, 5,10-methylenetetrahydropteroylglutamate reductase, 5-methylenetetrahydrofolate:NADP+ oxidoreductase, 5-methyltetrahydrofolate:(acceptor) oxidoreductase, 5-methyltetrahydrofolate:NAD oxidoreductase, 5-methyltetrahydrofolate:NAD+ oxidoreductase, 5-methyltetrahydrofolate:NADP+ oxidoreductase, AtMTHFR-1, EC 1.1.1.171, EC 1.1.1.68, EC 1.1.99.15, EC 1.7.99.5, HsMTHFR, MET13, methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase, methylenetetrahydrofolate reductase, methylenetetrahydrofolate reductase (NADPH), methylenetetrahydrofolic acid reductase, MetVF-type methylenetetrahydrofolate reductase, More, MTHFR, MTHFR2, N5,10-methylenetetrahydrofolate reductase, N5,N10-methylenetetrahydrofolate reductase, NADH:CH2-H4folate oxidoreductase, NapAB, reductase, methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate), reductase, methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide), respiratory nitrate reductase, type II-MTHFR

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.20 methylenetetrahydrofolate reductase [NAD(P)H]

Crystallization

Crystallization on EC 1.5.1.20 - methylenetetrahydrofolate reductase [NAD(P)H]

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determined at a resolution of 3.2 A
-
His-tagged wild-type and mutant E28Q
-
ligand-free mutant F223L and mutant F223L/E28Q in complex with methylenetetrahydrofolate, to 1.65 and 1.7 A resolution, respectively. folate is bound in a catalytically competent conformation, and L223 undergoes a conformational change similar to that observed for F223 in the E28Q-methylenetetrahydrofolate structure
mutant A177V, free and in complex with 5,10-dideazafolate analogue LY309887
-
hanging-drop vapor diffusion method. Structure of proteolyzed form of recombinant NapB at 1.25 A resolution
-
purified enzyme in complex with FAD and SAH, X-ray diffraction structure determination and analysis at 2.5 A resolution
hanging drop vapor diffusion method, using 0.1 M sodium acetate buffer (NaOAc, pH 4.3,4.5), 1 M lithium chloride, 10% (w/v) polyethylene glycol 6000, 10-20% (v/v) glycerol, and 2-5% (v/v) dioxane, at 20°C