methylenetetrahydrofolate dehydrogenase (NADP+)
Methylenetetrahydrofolate dehydrogenase dimer, Human
Identifiers
EC no.1.5.1.5
CAS no.9029-14-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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. 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.

Clinical significance

Mutations of the MTHFD1 gene may disrupt the activity of the enzyme and cause methylenetetrahydrofolate dehydrogenase 1 deficiency, also known as combined immunodeficiency and megaloblastic anemia with or without hyperhomocysteinemia (CIMAH).

Alternative names

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).

References

    • Hatefi Y, Osborn MJ, Kay LD, Huennekins FM (1957). "Hydroxymethyl tetrahydrofolic dehydrogenase". Journal of Biological Chemistry. 227 (2): 637–47. doi:10.1016/S0021-9258(18)70744-8. PMID 13462986.
    • Osborn MJ, Huennekens FM (1957). "Participation of anhydroleucovorin in the hydroxymethyl tetrahydrofolic dehydrogenase system". Biochimica et Biophysica 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". The Journal of Biological Chemistry. 237: 1982–8. doi:10.1016/S0021-9258(19)73970-2. PMID 14490085.
    • Yeh YC, Greenberg DM (1965). "Purification and properties of N5, N10-Methylenetetra-hydrofolate dehydrogenase of calf thymus". Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation. 105 (2): 279–91. doi:10.1016/s0926-6593(65)80152-7. PMID 4379024.


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