In enzymology, formyltetrahydrofolate dehydrogenase () is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are 10-formyltetrahydrofolate, oxidised nicotinamide adenine dinucleotide phosphate (NADP<sup>+</sup>), and water. Its products are tetrahydrofolic acid, carbon dioxide, reduced NADPH, and a proton.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 10-formyltetrahydrofolate:NADP+ oxidoreductase. Other names in common use include 10-formyl tetrahydrofolate:NADP oxidoreductase, 10-formyl-H2PtGlu:NADP oxidoreductase, 10-formyl-H4folate dehydrogenase, N10-formyltetrahydrofolate dehydrogenase, and 10-formyltetrahydrofolate dehydrogenase. This enzyme participates in one carbon pool by folate.
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .