Trichodiene synthase
| trichodiene synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.3.6 | ||||||||
| CAS no. | 101915-76-8 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a trichodiene synthase (EC 4.2.3.6) is an enzyme that catalyzes the chemical reaction
- trans,trans-farnesyl diphosphate trichodiene + diphosphate
Hence, this enzyme has one substrate, trans,trans-farnesyl diphosphate, and two products, and diphosphate.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, trichodiene-forming). Other names in common use include trichodiene synthetase, sesquiterpene cyclase, and trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase. This enzyme participates in terpenoid biosynthesis.
Structural studies[]
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1YJ4, 1YYQ, 1YYR, 1YYS, 1YYT, 1YYU, 2AEK, 2AEL, and 2AET.
References[]
- Hohn TM, Vanmiddlesworth F (1986). "Purification and characterization of the sesquiterpene cyclase trichodiene synthetase from Fusarium sporotrichioides". Arch. Biochem. Biophys. 251 (2): 756–61. doi:10.1016/0003-9861(86)90386-3. PMID 3800398.
- EC 4.2.3
- Enzymes of known structure
- EC 4.2 stubs