Trichodiene synthase
| trichodiene synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.3.6 | ||||||||
| CAS number | Template:CAS | ||||||||
| 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 / EGO | ||||||||
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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, trichodiene 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
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