Substrate specificity of the CYC2 enzyme from Kitasatospora griseola: production of sclarene, biformene, and novel bicyclic diterpenes by the enzymatic reactions of labdane- and halimane-type diterpene diphosphates

Substrate specificity of the CYC2 enzyme from Kitasatospora griseola: production of sclarene, biformene, and novel bicyclic diterpenes by the enzymatic reactions of labdane- and halimane-type diterpene diphosphates

The enzymatic reaction of copalyl diphosphate (CDP), ent-CDP, syn-CDP, and tuberculosinyl diphosphate with the CYC2 enzyme from Kitasatospora griseola afforded sclarene, biformene, and novel diterpenes having a buta-1,3-diene moiety in the side chain. The substrate specificity of the CYC2 is discuss...

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Veröffentlicht in:Tetrahedron letters 2010-01, Vol.51 (1), p.125-128
Hauptverfasser: Nakano, Chiaki, Hoshino, Tsutomu, Sato, Tsutomu, Toyomasu, Tomonobu, Dairi, Tohru, Sassa, Takeshi
Format: Artikel
Sprache:eng
Schlagworte:
Biformene
Diterpenes
Enzymatic synthesis
Kitasatospora
Sclarene
Unnatural natural product
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Zusammenfassung:The enzymatic reaction of copalyl diphosphate (CDP), ent-CDP, syn-CDP, and tuberculosinyl diphosphate with the CYC2 enzyme from Kitasatospora griseola afforded sclarene, biformene, and novel diterpenes having a buta-1,3-diene moiety in the side chain. The substrate specificity of the CYC2 is discussed.
ISSN:0040-4039
1873-3581
DOI:10.1016/j.tetlet.2009.10.110