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
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
1.5.1.53 methylenetetrahydrofolate reductase (NADPH)Advanced search results
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results (Inhibitors
Inhibitors on EC 1.5.1.53 - methylenetetrahydrofolate reductase (NADPH)
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(S)-SKI-72
presence of (S)-SKI-72 leads to a Tm shift of approximately 10 degrees
NADPH
-
substrate inhibition. NADPH and S-adenosyl-L-methionine play antagonistic roles in the allosteric regulation, with NADPH recruiting active forms of the enzyme and S-adenosyl-L-methionine recruiting inactive forms. Enzyme can adopt two states, R and T. NADPH and S-adenosyl-L-methionine exhibit antagonistic binding to a given subunit, so that occupancy by one ligand decreases or abolishes affinity for the other ligand. Within a given state, the subunits do not interact with each other. R-T transitions occur between all similarly ligated states
S-adenosyl-L-methionine
presence of S-adenosyl-L-methionine leads to a Tm shift of about 4 degrees
S-adenosyl-L-methionine
-
NADPH and S-adenosyl-L-methionine play antagonistic roles in the allosteric regulation, with NADPH recruiting active forms of the enzyme and S-adenosyl-L-methionine recruiting inactive forms. Enzyme can adopt two states, R and T. NADPH and S-adenosyl-L-methionine exhibit antagonistic binding to a given subunit, so that occupancy by one ligand decreases or abolishes affinity for the other ligand. Within a given state, the subunits do not interact with each other. R-T transitions occur between all similarly ligated states
