5-formyltetrahydrofolate cyclo-ligase

MTHFS
Identifiers
Aliases	MTHFS, HsT19268, 5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), methenyltetrahydrofolate synthetase, NEDMEHM
External IDs	OMIM: 604197; MGI: 3780550; GeneCards: MTHFS
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	3HY4, 3HXT, 3HY3, 3HY6
Enzyme activity
Gene location (Human)
Chr.	Chromosome 15 (human)
End	79,897,379 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	88,602,349 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; monocyte; ; blood; ; duodenum; ; body of pancreas; ; renal cortex; ; pituitary gland; ; human kidney; ; C1 segment; ; anterior pituitary;
	Top expressed in
	right kidney; ; proximal tubule; ; granulocyte; ; exocrine gland; ; hepatobiliary system; ; liver; ; neural layer of retina; ; human kidney; ; white adipose tissue; ; lens;
	More reference expression data
	n/a
Gene ontology
Molecular function	folic acid binding; ligase activity; ATP binding; metal ion binding; nucleotide binding; 5-formyltetrahydrofolate cyclo-ligase activity;
Cellular component	mitochondrial matrix; cytoplasm; cytosol; mitochondrion;
Biological process	tetrahydrofolate metabolic process; glutamate metabolic process; formate metabolic process; folic acid-containing compound biosynthetic process; tetrahydrofolate interconversion; folic acid catabolic process; folic acid metabolic process;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	10588
	100039707
	ENSG00000136371
	ENSMUSG00000079427
	P49914
	n/a
	NM_001199758; NM_006441
	NM_001128601; NM_001359992
	NP_001186687; NP_006432
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

Search
PMC	articles
PubMed	articles
NCBI	proteins

5-Formyltetrahydrofolate cyclo-ligase
5-Formyltetrahydrofolate cyclo-ligase
Identifiers
EC no.	6.3.3.2
CAS no.	37318-64-2
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
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

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 PDB: 1SBQ, PDB: 1SOU, PDB: 1U3F, PDB: 1U3G, and PDB: 2JCB.

Human gene

The human version of the enzyme is known as the 5,10-methenyltetrahydrofolate synthetase, gene symbol MTHFS.

Role in pathology

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

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000136371 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000079427 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse 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.

This EC 6.3 enzyme-related article is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000136371 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000079427 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

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v t e Enzymes: CO CS and CN ligases (EC 6.1-6.3)
6.1: Carbon-Oxygen	Aminoacyl tRNA synthetase Alanine Arginine Asparagine Aspartate Cysteine D-Alanine—poly(phosphoribitol) ligase Glutamate Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine
6.2: Carbon-Sulfur	(2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase 2-furoate—CoA ligase 3-alpha,7-alpha-dihydroxy-5-beta-cholestanate—CoA ligase 3-hydroxybenzoate—CoA ligase 3-hydroxypropionyl-CoA synthase 4-chlorobenzoate—CoA ligase 4-Coumarate-CoA ligase 4-hydroxybenzoate—CoA ligase 6-carboxyhexanoate—CoA ligase Acetate—ACP ligase Acetate—CoA ligase (ADP-forming) Acetoacetate—CoA ligase Acetyl—CoA synthetase Acid—CoA ligase (GDP-forming) Anthranilate—CoA ligase Arachidonate—CoA ligase Benzoate—CoA ligase Biotin—CoA ligase (butirosin acyl-carrier protein)—L-glutamate ligase Butyrate—CoA ligase Cholate—CoA ligase Citrate—CoA ligase (citrate (pro-3S)-lyase) ligase Dicarboxylate—CoA ligase Glutarate—CoA ligase Long-chain-fatty-acid—ACP ligase Long-chain-fatty-acid—CoA ligase Malate—CoA ligase Malonate—CoA ligase o-Succinylbenzoate—CoA ligase Oxalate—CoA ligase Phenylacetate—CoA ligase Phytanate—CoA ligase Propionate—CoA ligase Succinate—CoA ligase (ADP-forming) Succinate—CoA ligase (GDP-forming) Succinyl—CoA synthetase trans-Feruloyl—CoA synthase
6.3: Carbon-Nitrogen	Glutamine synthetase Ubiquitin ligase Cullin Von Hippel–Lindau tumor suppressor UBE3A Mdm2 Anaphase-promoting complex UBR1 Glutathione synthetase CTP synthetase Adenylosuccinate synthase Argininosuccinate synthase Holocarboxylase synthetase GMP synthase Asparagine synthetase Carbamoyl phosphate synthetase I II Glutamate–cysteine ligase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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Structural studies

Human gene

Role in pathology

References