Department of Chemical and Biomolecular Engineering, University of California-Los Angeles, Los Angeles, California, USA.
Nat Chem Biol. 2012 Mar 11;8(4):331-3. doi: 10.1038/nchembio.912.
Iterative highly reducing polyketide synthases from filamentous fungi are the most complex and enigmatic type of polyketide synthase discovered to date. Here we uncover an unusual degree of programming by the hypothemycin highly reducing polyketide synthase, in which a single ketoreductase domain shows stereospecificity that is controlled by substrate length. Mapping of the structural domains responsible for this feature allowed for the biosynthesis of an unnatural diastereomer of the natural product dehydrozearalenol.
丝状真菌中的迭代高度还原聚酮合酶是迄今为止发现的最复杂和最神秘的聚酮合酶类型。在这里，我们揭示了 Hypothemycin 高度还原聚酮合酶的一种不同寻常的编程方式，其中单个酮还原酶结构域显示出立体特异性，这种特异性由底物长度控制。负责这一特征的结构域的作图使得能够生物合成天然产物脱氢玉米赤霉醇的非天然对映异构体。
