5-formyltetrahydrofolate cyclo-ligase

5-formyltetrahydrofolate cyclo-ligase
Identifiers
Aliases	methenyl-THF synthetase5,10-methenyltetrahydrofolate synthetase5-formyltetrahydrofolate cyclo-ligase (ADP-forming)5-Formyltetrahydrofolate cyclodehydraseformyltetrahydrofolic cyclodehydrase
External IDs	OMIM: 604197 GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	10588	n/a
Ensembl	ENSG00000136371	n/a
UniProt	n a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search		n/a
Wikidata
View/Edit Human

5-formyltetrahydrofolate cyclo-ligase
Identifiers
EC no.	6.3.3.2
CAS no.	37318-64-2
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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a 5-formyltetrahydrofolate cyclo-ligase (EC 6.3.3.2) is an enzyme that catalyzes the chemical reaction

ATP + 5-formyltetrahydrofolate (folinic acid) $\rightleftharpoons$ ADP + phosphate + 5,10-methenyltetrahydrofolate

Thus, the two substrates of this enzyme are ATP and 5-formyltetrahydrofolate, whereas its 3 products are ADP, phosphate, and 5,10-methenyltetrahydrofolate.

This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic name of this enzyme class is 5-formyltetrahydrofolate cyclo-ligase (ADP-forming). Other names in common use include 5,10-methenyltetrahydrofolate synthetase (MTHFS), formyltetrahydrofolic cyclodehydrase, and 5-formyltetrahydrofolate cyclodehydrase. This enzyme participates in one carbon pool by folate.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1SBQ, 1SOU, 1U3F, 1U3G, and 2JCB.

Role in pathology

Mutations of the MTHFS gene cause the disease 5,10-methenyltetrahydrofolate synthetase deficiency.

References

• Greenberg DM, Wynston LK, Nagabhushanan A (1965). "Further studies on N5-formyltetrahydrofolic acid cyclodehydrase". Biochemistry. 4 (9): 1872–1878. doi:10.1021/bi00885a026.