Bornyl diphosphate synthase: Structure and strategy for carbocation manipulation by a terpenoid cyclase
Bornyl diphosphate synthase: Structure and strategy for carbocation manipulation by a terpenoid cyclase
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DOI：
10.1073/pnas.232591099
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发表时间：
2002-11-26
影响因子：
11.1
通讯作者：
Christianson, DW
中科院分区：
文献类型：
--
作者：
Whittington, DA;Wise, ML;Christianson, DW
报道了二聚(+)-龙脑二磷酸合成酶的X射线晶体结构，该酶是丹参中的一种需要金属的单萜环化酶，分辨率为2.0埃。每个单体都含有两个α-螺旋结构域：C-末端结构域催化二磷酸香叶基的环化，定向和稳定多种反应性碳正离子中间体；N-末端结构域没有明确的功能定义，尽管它的N-末端在催化过程中覆盖了C-末端结构域中的活性部位。具有氮杂类似物的底物和碳正离子中间体的络合物，以及与焦磷酸盐和龙脑基二磷酸的络合物，提供了萜类环化级联的“快照”。
The x-ray crystal structure of dimeric (+)-bornyl diphosphate synthase, a metal-requiring monoterpene cyclase from Salvia officinalis, is reported at 2.0-Angstrom resolution. Each monomer contains two alpha-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates; the N-terminal domain has no clearly defined function, although its N terminus caps the active site in the C-terminal domain during catalysis. Structures of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with pyrophosphate and bornyl diphosphate, provide "snapshots" of the terpene cyclization cascade.