Formyltetrahydrofolate dehydrogenase

In enzymology, a formyltetrahydrofolate dehydrogenase (EC 1.5.1.6) is an enzyme that catalyzes the chemical reaction

10-formyltetrahydrofolate + NADP⁺ + H₂O ${\displaystyle \rightleftharpoons }$ tetrahydrofolate + CO₂ + NADPH + H⁺

The 3 substrates of this enzyme are 10-formyltetrahydrofolate, NADP⁺, and H₂O, whereas its 4 products are tetrahydrofolate, CO₂, NADPH, and H⁺.

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.

Structural studies[]

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1S3I, 2BW0, 2CFI, 2CQ8, 2O2P, 2O2Q, and 2O2R.

References[]

• Kutzbach C, Stokstad EL (1968). "Partial purification of a 10-formyl-tetrahydrofolate: NADP oxidoreductase from mammalian liver". Biochem. Biophys. Res. Commun. 30 (2): 111–7. doi:10.1016/0006-291X(68)90456-7. PMID 4384443.