Methylenetetrahydrofolate dehydrogenase (NAD+)
| methylenetetrahydrofolate dehydrogenase (NAD+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
In enzymology, a methylenetetrahydrofolate dehydrogenase (NAD+) (EC 1.5.1.15) is an enzyme that catalyzes a chemical reaction.[1]
- 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.[2]
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1EDZ and 1EE9.[3]
References
- ^ "1.5.1.15: methylenetetrahydrofolate dehydrogenase (NAD+) - BRENDA Enzyme Database". www.brenda-enzymes.org. Retrieved 2023-02-18.
- ^ "Methylenetetrahydrofolate dehydrogenase NAD". LOINC. Retrieved 2023-02-18.
- ^ 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. PMID 4153026.
