Institute for Organic Chemistry and BMWZ, Leibniz Universität Hannover, Schneiderberg 38, 30167, Hannover, Germany.
Current address: The Molecular Biology Institute, UCLA, Los Angeles, CA, 90095-1570, USA.
Angew Chem Int Ed Engl. 2021 May 10;60(20):11423-11429. doi: 10.1002/anie.202100969. Epub 2021 Apr 8.
The polyketide synthase (PKS)-like protein TerB, consisting of inactive dehydratase, inactive C-methyltransferase, and functional ketoreductase domains collaborates with the iterative non reducing PKS TerA to produce 6-hydroxymellein, a key pathway intermediate during the biosynthesis of various fungal natural products. The catalytically inactive dehydratase domain of TerB appears to mediate productive interactions with TerA, demonstrating a new mode of trans-interaction between iterative PKS components.
聚酮合酶（PKS）样蛋白 TerB 由失活的脱水酶、失活的 C-甲基转移酶和功能酮还原酶结构域组成，与迭代非还原 PKS TerA 协同作用，生成 6-羟甲氧基麦角甾酮，这是真菌天然产物生物合成过程中的一个关键途径中间体。TerB 的催化失活脱水酶结构域似乎介导了与 TerA 的有效相互作用，证明了迭代 PKS 组件之间的新型跨相互作用模式。
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