Formimidoyltetrahydrofolate cyclodeaminase
| formimidoyltetrahydrofolate cyclodeaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.1.4 | ||||||||
| CAS no. | 9032-05-7 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) is an enzyme that catalyzes the chemical reaction
- 5-formimidoyltetrahydrofolate 5,10-methenyltetrahydrofolate + NH3
Hence, this enzyme has one substrate, 5-formimidoyltetrahydrofolate, and two products, 5,10-methenyltetrahydrofolate and NH3.[1]
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing 5,10-methenyltetrahydrofolate-forming). Other names in common use include formiminotetrahydrofolate cyclodeaminase, and 5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing). This enzyme participates in folate metabolism by catabolising histidine and adding to the C1-tetrahydrofolate pool.
In mammals, this enzyme can be found as part of a bifunctional enzyme in a single polypeptide with glutamate formimidoyltransferase (EC 2.1.2.5), the enzyme activity that catalyses the previous step in the histidine catabolic pathway.[2] This arrangement allows the 5-formimidoyltetrahydrofolate intermediate to move directly from one active site to another without being released into solution, in a process called substrate channeling.[3]
Structural studies
[edit]As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1O5H, 1TT9, and 2PFD.
References
[edit]- ^ Rabinowitz JC; Pricer WE (1956). "Formiminotetrahydrofolic acid and methenyltetrahydrofolic acid as intermediates in the formation of N10-formyltetrahydrofolic acid". J. Am. Chem. Soc. 78 (21): 5702–5704. doi:10.1021/ja01602a073.
- ^ MacKenzie RE, Aldridge M, Paquin J (10 October 1980). "The bifunctional enzyme formiminotransferase-cyclodeaminase is a tetramer of dimers". J. Biol. Chem. 255 (19): 9474–8. doi:10.1016/S0021-9258(19)70586-9. PMID 7410436.
- ^ Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A (2000). "The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme". Structure. 8 (1): 35–46. doi:10.1016/S0969-2126(00)00078-2. PMID 10673422.
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