Mechanistic Characterization of Two Chimeric Sesterterpene Synthases from Penicillium
Mechanistic Characterization of Two Chimeric Sesterterpene Synthases from Penicillium
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DOI：
10.1002/chem.201702766
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发表时间：
2017-07-26
影响因子：
4.3
通讯作者：
Dickschat, Jeroen S.
中科院分区：
文献类型：
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作者：
Mitsuhashi, Takaaki;Rinkel, Jan;Dickschat, Jeroen S.
通过标记实验，对青霉菌两种具有双功能的双烯丙基转移酶（PT）和萜烯合成酶（TPS）的产物进行了结构表征，并对其机制进行了详细的研究。新的和先前表征的酶的TPS结构域的系统发育分析揭示了六个不同的分支。来自同一进化支的酶催化一个共同的初始环化步骤，这表明从氨基酸序列预测结构的潜力。
The products of two bifunctional fungal sesterterpene synthases (StTPS), with prenyl transferase (PT) and terpene synthase (TPS) domains from Penicillium, were structurally characterized and their mechanisms studied in detail by labeling experiments. A phylogenetic analysis of the TPS domains of the new and previously characterized enzymes revealed six distinct clades. Enzymes from the same clade catalyze a common initial cyclization step, which suggests the potential for structural predictions from amino acid sequences.