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, methylenetetrahydrofolate dehydrogenase (NAD+) (EC 1.5.1.15) is an enzyme that catalyzes the chemical reaction.[1]
The two substrates of this enzyme are 5,10-methylenetetrahydrofolate and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are 5,10-methenyltetrahydrofolate, reduced NADH, and a proton.[2][3]
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.[4]
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1EDZ and 1EE9.[5]
References
- ^ "1.5.1.15: methylenetetrahydrofolate dehydrogenase (NAD+) - BRENDA Enzyme Database". www.brenda-enzymes.org. Retrieved 2023-02-18.
- ^ Enzyme 1.5.1.15 at KEGG Pathway Database.
- ^ 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. doi:10.1016/S0021-9258(19)42355-7. PMID 4153026.
- ^ "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.