Methylenetetrahydrofolate dehydrogenase (NAD+)
methylenetetrahydrofolate dehydrogenase (NAD+) | |||||||||
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Identifiers | |||||||||
EC no. | 1.5.1.15 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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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+ 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.
- EC 1.5.1
- NADH-dependent enzymes
- Enzymes of known structure
- Oxidoreductase stubs