Terpentedienyl-diphosphate synthase (EC 5.5.1.15, terpentedienol diphosphate synthase, Cyc1, clerodadienyl diphosphate synthase) is an enzyme with systematic name terpentedienyl-diphosphate lyase (decyclizing).[1][2][3] This enzyme catalyses the following chemical reaction
| Terpentedienyl-diphosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.5.1.15 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- geranylgeranyl diphosphate terpentedienyl diphosphate
This enzyme requires Mg2+.
References edit
- ^ Dairi T, Hamano Y, Kuzuyama T, Itoh N, Furihata K, Seto H (October 2001). "Eubacterial diterpene cyclase genes essential for production of the isoprenoid antibiotic terpentecin". Journal of Bacteriology. 183 (20): 6085–94. doi:10.1128/jb.183.20.6085-6094.2001. PMC 99688. PMID 11567009.
- ^ Hamano Y, Kuzuyama T, Itoh N, Furihata K, Seto H, Dairi T (October 2002). "Functional analysis of eubacterial diterpene cyclases responsible for biosynthesis of a diterpene antibiotic, terpentecin". The Journal of Biological Chemistry. 277 (40): 37098–104. doi:10.1074/jbc.m206382200. PMID 12138123.
- ^ Eguchi T, Dekishima Y, Hamano Y, Dairi T, Seto H, Kakinuma K (July 2003). "A new approach for the investigation of isoprenoid biosynthesis featuring pathway switching, deuterium hyperlabeling, and 1H NMR spectroscopy. The reaction mechanism of a novel streptomyces diterpene cyclase". The Journal of Organic Chemistry. 68 (14): 5433–8. doi:10.1021/jo026728a. PMID 12839434.
External links edit
- Terpentedienyl-diphosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
