Formate—dihydrofolate ligase
| formate—dihydrofolate ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.4.17 | ||||||||
| CAS number | 123303-25-3 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a formate—dihydrofolate ligase (EC 6.3.4.17) is an enzyme that catalyzes the chemical reaction
- ATP + formate + dihydrofolate ADP + phosphate + 10-formyldihydrofolate
The 3 substrates of this enzyme are ATP, formate, and dihydrofolate, whereas its 3 products are ADP, phosphate, and 10-formyldihydrofolate.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is formate:dihydrofolate ligase (ADP-forming). Other names in common use include formyltransferase, dihydrofolate, dihydrofolate formyltransferase, and formyl dihydrofolate synthase.
References
Further reading
- Drake JC, Baram J, Allegra CJ (1990). "Isolation and characterization of a novel dihydrofolate formylating enzyme from human MCF-7 breast cancer cells". Biochem. Pharmacol. 39 (3): 615–8. doi:10.1016/0006-2952(90)90073-T. PMID 2306274.
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