Mitsuhashi Takaaki, Rinkel Jan, Okada Masahiro, Abe Ikuro, Dickschat Jeroen S
Graduate School of Pharmaceutical Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Kekulé-Institute of Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Straße 1, 53121, Bonn, Germany.
Chemistry. 2017 Jul 26;23(42):10053-10057. doi: 10.1002/chem.201702766. Epub 2017 Jul 3.
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.
对来自青霉的具有异戊烯基转移酶（PT）和萜烯合酶（TPS）结构域的两种双功能真菌倍半萜合酶（StTPS）的产物进行了结构表征，并通过标记实验对其机制进行了详细研究。对新的和先前已表征的酶的TPS结构域进行系统发育分析，揭示了六个不同的进化枝。来自同一进化枝的酶催化一个共同的初始环化步骤，这表明从氨基酸序列进行结构预测具有可能性。
