Formyltetrahydrofolate dehydrogenase

From Wikipedia, the free encyclopedia

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

 
 
H2O
H+
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
H2O
H+
 
+ CO2 + NADPH
 

The three substrates of this enzyme are 10-formyltetrahydrofolate, oxidised nicotinamide adenine dinucleotide phosphate (NADP+), and water. Its products are tetrahydrofolic acid, carbon dioxide, reduced NADPH, and a proton.[1][2]

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

Related Articles

Wikiwand AI