Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.5.1.53: methylenetetrahydrofolate reductase (NADPH)

This is an abbreviated version!
For detailed information about methylenetetrahydrofolate reductase (NADPH), go to the full flat file.

Reaction

5-methyltetrahydrofolate
+
NADP+
=
5,10-methylenetetrahydrofolate
+
NADPH
+
H+

Synonyms

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-methyltetrahydrofolate:(acceptor) oxidoreductase, MET13, methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate) reductase, methylenetetrahydrofolate reductase, methylenetetrahydrofolate reductase (NADPH2), methylenetetrahydrofolic acid reductase, MTHFR, N5,10-methylenetetrahydrofolate reductase, N5,N10-methylenetetrahydrofolate reductase

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.53 methylenetetrahydrofolate reductase (NADPH)

Crystallization

Crystallization on EC 1.5.1.53 - methylenetetrahydrofolate reductase (NADPH)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of human MTHFR at 2.5 A resolution reveals a unique architecture, appending the well-conserved catalytic TIM-barrel to a eukaryote-only SAM-binding domain. The latter domain provides the predominant interface for MTHFR homo-dimerization and positions the N-terminal serine-rich phosphorylation region near the C-terminal SAM-binding domain. MTHFR phosphorylation, identified on 11 N-terminal residues (16 in total), increases sensitivity to SAM binding and inhibition. The 25-amino-acid inter-domain linker enables conformational plasticity and may be a key mediator of SAM regulation