Sativene (1) and seco-sativene are an important family of fungal sesquiterpenoids that feature unique tricyclo[4.4.0.01,7]decane and bicyclo[3.2.1]octane skeletons, respectively. Herein, we identify a three-enzyme cassette: SatA cyclizes farnesyl diphosphate (FPP) to form compound 1; CYP450 SatB catalyzes C14–C15 dihydroxylations and subsequent bond cleavage; and reductase SatC regioselectively reduces
Sativene ( 1 ) 和seco -sativene 是真菌
倍半萜类化合物的重要家族,分别具有独特的
三环[4.4.0.0 1,7 ]
癸烷和
双环[3.2.1]辛烷骨架。在此,我们鉴定了一个三酶盒: SatA 环化法呢基二
磷酸 (FPP) 形成化合物1 ; CYP450 SatB 催化 C14–C15 二羟基化和随后的键断裂;还原酶 SatC 区域选择性地还原 C14 醛并介导
半缩醛闭环以生成 prehelminthosporol ( 2 )。我们的研究结果阐明了sativene的合成步骤及其氧化转化为seco -sativene的过程。