A ThDP-dependent enzymatic carboligation reaction involved in Neocarazostatin A tricyclic carbazole formation
A ThDP-dependent enzymatic carboligation reaction involved in Neocarazostatin A tricyclic carbazole formation
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DOI：
10.1039/c6ob01651k
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发表时间：
2016-01-01
影响因子：
3.2
通讯作者：
Yu, Yi
中科院分区：
文献类型：
--
作者：
Su, Li;Lv, Meinan;Yu, Yi
虽然已经确定了Neocarazostatin A（1）的生物合成途径，但咔唑环组装的详细酶促反应仍然在很大程度上未知。我们在这里证明，NzsH，一个假定的硫胺素二磷酸依赖性酶，可以催化吲哚-3-丙酮酸和丙酮酸之间的偶联反应，产生β-酮酸中间体。因此，我们的研究结果揭示了细菌三环咔唑生物碱的不寻常的生物合成途径的进一步表征。
Although the biosynthetic pathway of Neocarazostatin A (1) has been identified, the detailed enzymatic reactions underlying the assembly of the carbazole ring still remain largely unknown. We demonstrate here that NzsH, a putative thiamine diphosphate dependent enzyme, can catalyze an acyloin coupling reaction between indole-3-pyruvate and pyruvate to generate a beta-ketoacid intermediate. Our findings thus shed light on further characterization of the unusual biosynthetic pathway of the bacterial tricyclic carbazole alkaloids.