Methylenetetrahydrofolate dehydrogenase (NADP+)

In enzymology, a methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) is an enzyme that catalyzes the chemical reaction

5,10-methylenetetrahydrofolate + NADP⁺ 5,10-methenyltetrahydrofolate + NADPH + H⁺

Thus, the two substrates of this enzyme are 5,10-methylenetetrahydrofolate and NADP⁺, whereas its 3 products are 5,10-methenyltetrahydrofolate, NADPH, 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:NADP+ oxidoreductase. Other names in common use include N5,N10-methylenetetrahydrofolate dehydrogenase, 5,10-methylenetetrahydrofolate:NADP oxidoreductase, 5,10-methylenetetrahydrofolate dehydrogenase, methylenetetrahydrofolate dehydrogenase, and methylenetetrahydrofolate dehydrogenase (NADP). This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1A4I, 1DIA, 1DIB, 1DIG, 1LU9, 1LUA, 2C2X, and 2C2Y.

References

• HATEFI Y, OSBORN MJ, KAY LD, HUENNEKENS FM (1957). "Hydroxymethyl tetrahydrofolic dehydrogenase". J. Biol. Chem. 227 (2): 637–47. PMID 13462986. 
• OSBORN MJ, HUENNEKENS FM (1957). "Participation of anhydroleucovorin in the hydroxymethyl tetrahydrofolic dehydrogenase system". Biochim. Biophys. Acta. 26 (3): 646–7. doi:10.1016/0006-3002(57)90117-8. PMID 13499428. 
• RAMASASTRI BV, BLAKLEY RL (1962). "5,10-Methylenetetrahydrofolic dehydrogenase from bakers' yeast. I Partial purification and some properties". J. Biol. Chem. 237: 1982–8. PMID 14490085. 
• Yeh YC, Greenberg DM (1965). "Purification and properties of N5, N10-Methylenetetra-hydrofolate dehydrogenase of calf thymus". Biochim. Biophys. Acta. 105 (2): 279–91. doi:10.1016/s0926-6593(65)80152-7. PMID 4379024.