5-formyltetrahydrofolate cyclo-ligase
Identifiers
Aliasesmethenyl-THF synthetase5,10-methenyltetrahydrofolate synthetase5-formyltetrahydrofolate cyclo-ligase (ADP-forming)5-Formyltetrahydrofolate cyclodehydraseformyltetrahydrofolic cyclodehydrase
External IDsOMIM: 604197 GeneCards:
Orthologs
SpeciesHumanMouse
Entrez

10588

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Ensembl

ENSG00000136371

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UniProt

n
a

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RefSeq (mRNA)

n/a

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RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed search[1]n/a
Wikidata
View/Edit Human
5-Formyltetrahydrofolate cyclo-ligase
Identifiers
EC no.6.3.3.2
CAS no.37318-64-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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) 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

  1. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • Greenberg DM, Wynston LK, Nagabhushanan A (1965). "Further studies on N5-formyltetrahydrofolic acid cyclodehydrase". Biochemistry. 4 (9): 1872–1878. doi:10.1021/bi00885a026.


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