Methenyltetrahydrofolate cyclohydrolase
In enzymology, a methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) is an enzyme that catalyzes the chemical reaction
- 5,10-methenyltetrahydrofolate + H2O 10-formyltetrahydrofolate
| methenyltetrahydrofolate cyclohydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Methenyltetrahydrofolate cyclohydrolase dimer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 3.5.4.9 | ||||||||
| CAS number | 9027-97-8 | ||||||||
| 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 | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are 5,10-methenyltetrahydrofolate and H2O, whereas its product is 10-formyltetrahydrofolate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines.
This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.
Synonyms
The systematic name of this enzyme class is 5,10-methenyltetrahydrofolate 5-hydrolase (decyclizing).
Other names in common use include:
- Citrovorum factor cyclodehydrase
- cyclohydrolase
- formyl-methenyl-methylenetetrahydrofolate synthetase (combined).
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1A4I, 1DIA, 1DIB, 1DIG, 2C2X, and 2C2Y.
References
- Rabinowitz JC, Pricer WE (1956). "The enzymatic synthesis of N10-formyltetrahydrofolic acid and its role in ATP formation during formiminoglycine degradation". J. Am. Chem. Soc. 78 (16): 4176–4178. doi:10.1021/ja01597a094.
- Tabor H, Wyngarden L (July 1959). "The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid". The Journal of Biological Chemistry. 234 (7): 1830–46. PMID 13672973.