Life Sciences Institute, University of Michigan, Ann Arbor, Michigan, USA 48109.
Nat Prod Rep. 2018 Oct 17;35(10):1082-1096. doi: 10.1039/c8np00058a.
Covering: up to the end of 2018 Polyketides are a valuable source of bioactive and clinically important molecules. The biosynthesis of these chemically complex molecules has led to the discovery of equally complex polyketide synthase (PKS) pathways. Crystallography has yielded snapshots of individual catalytic domains, di-domains, and multi-domains from a variety of PKS megasynthases, and cryo-EM studies have provided initial views of a PKS module in a series of defined biochemical states. Here, we review the structural and biochemical results that shed light on the protein-protein interactions critical to catalysis by PKS systems with an embedded acyltransferase. Interactions include those that occur both within and between PKS modules, as well as with accessory enzymes.
截至 2018 年底，聚酮类化合物是生物活性和临床重要分子的宝贵来源。这些化学结构复杂的分子的生物合成导致了同样复杂的聚酮合酶（PKS）途径的发现。晶体学已经提供了来自各种 PKS 巨合酶的单个催化结构域、二结构域和多结构域的快照，冷冻电镜研究提供了一系列定义明确的生化状态下 PKS 模块的初步视图。在这里，我们回顾了结构和生化结果，这些结果阐明了对于嵌入酰基转移酶的 PKS 系统催化至关重要的蛋白质-蛋白质相互作用。相互作用包括发生在 PKS 模块内部和之间的相互作用，以及与辅助酶的相互作用。
