Reactome | MTHFD1 dimer ligates HCOOH to THFPG to form 10-formyl-THFPG

MTHFD1 dimer ligates HCOOH to THFPG to form 10-formyl-THFPG

Stable Identifier

R-HSA-200711

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

Synonyms

THF polyglutamate + formate + ATP => 10-formylTHF polyglutamate + ADP + orthophosphate

ReviewStatus

5/5

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MTHFD1 dimer ligates HCOOH to THFPG to form 10-formyl-THFPG

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The formate-tetrahydrofolate ligase activity of the trifunctional MTHFD1 enzyme catalyzes the reaction of THF polyglutamate, formate, and ATP to form 10-formylTHF polyglutamate, ADP, and orthophosphate. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).

Literature References

PubMed ID	Title	Journal	Year
3053686	Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. MacKenzie, RE, Rozen, R, Hum, DW, Bell, AW	J Biol Chem	1988
3871768	C1-Tetrahydrofolate synthase from rabbit liver. Structural and kinetic properties of the enzyme and its two domains. Schuster, B, Villar, E, Schirch, V, Peterson, D	J Biol Chem	1985