| cycloartenol synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.99.8 | ||||||||
| CAS no. | 9075-25-6 | ||||||||
| 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 cycloartenol synthase (EC 5.4.99.8) is an enzyme that catalyzes the chemical reaction
- (S)-2,3-epoxysqualene cycloartenol
Hence, this enzyme has one substrate, (S)-2,3-epoxysqualene, and one product, cycloartenol.
This enzyme is an oxidosqualene cyclase and belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. This enzyme participates in biosynthesis of steroids.
Nomenclature
The systematic name of this enzyme class is:
- (S)-2,3-epoxysqualene mutase (cyclizing, cycloartenol-forming).
Other names in common use include:
- 2,3-epoxysqualene cycloartenol-cyclase
- squalene-2,3-epoxide-cycloartenol cyclase
- 2,3-epoxysqualene cycloartenol-cyclase
- 2,3-epoxysqualene-cycloartenol cyclase
- 2,3-oxidosqualene-cycloartenol cyclase
References
- Rees HH, Goad LJ, Goodwin TW (1969). "2,3-oxidosqualene cycloartenol cyclase from Ochromonas malhamensis". Biochim. Biophys. Acta. 176 (4): 892–4. doi:10.1016/0005-2760(69)90274-4. PMID 5797101.
This page was last edited on 22 February 2024, at 01:48