Methylenetetrahydrofolate dehydrogenase (NAD+)
methylenetetrahydrofolate dehydrogenase (NAD+) | |||||||||
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Identifiers | |||||||||
EC number | 1.5.1.15 | ||||||||
CAS number | 82062-90-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a methylenetetrahydrofolate dehydrogenase (NAD+) (EC 1.5.1.15) is an enzyme that catalyzes the chemical reaction
- 5,10-methylenetetrahydrofolate + NAD+ 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
- 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. PMID 4153026.