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In enzymology, a methylenetetrahydrofolate dehydrogenase (NAD) (EC 1.5.1.15) is an enzyme that catalyzes a chemical reaction.

5,10-methylenetetrahydrofolate + NAD ${\displaystyle \rightleftharpoons }$ 5,10-methenyltetrahydrofolate + NADH + H

Thus, the two substrates of this enzyme are 5,10-methylenetetrahydrofolate and NAD, whereas its 3 products are 5,10-methenyltetrahydrofolate, NADH, and H.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:NAD oxidoreductase. This enzyme is also called methylenetetrahydrofolate dehydrogenase (NAD). This enzyme participates in one carbon pool by folate.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1EDZ and 1EE9.

References

1. "1.5.1.15: methylenetetrahydrofolate dehydrogenase (NAD+) - BRENDA Enzyme Database". www.brenda-enzymes.org. Retrieved 2023-02-18.
2. "Methylenetetrahydrofolate dehydrogenase NAD". LOINC. Retrieved 2023-02-18.
3. Bank, RCSB Protein Data. "RCSB PDB - 1CKM: STRUCTURE OF TWO DIFFERENT CONFORMATIONS OF MRNA CAPPING ENZYME IN COMPLEX WITH GTP". www.rcsb.org. Retrieved 2023-02-18.

• Moore MR, O'Brien WE, Ljungdahl LG (1974). "Purification and characterization of nicotinamide adenine dinucleotide-dependent methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum". J. Biol. Chem. 249 (16): 5250–3. doi:10.1016/S0021-9258(19)42355-7. PMID 4153026.

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