Noncanonical Functions of Ketosynthase Domains in Type I Polyketide Synthases.

IF 2.6 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
ChemBioChem Pub Date : 2024-10-21 DOI:10.1002/cbic.202400751
Yuqiong Zhao, Wenyu Zhang, Wen Liu, Zhijun Tang
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引用次数: 0

Abstract

Modular type I polyketide synthases (PKSs) are remarkable molecular machines that can synthesize structurally complex polyketide natural products with a wide range of biological activities. In these molecular machines, ketosynthase (KS) domains play a central role, typically by catalyzing decarboxylative Claisen condensation for polyketide chain extension. Noncanonical KS domains with catalytic functions rather than Claisen condensation have increasingly been evidenced, further demonstrating the capability of type I PKSs for structural diversity. This review provides an overview of the reactions involving unusual KS activities, including PKS priming, acyl transfer, Dieckmann condensation, Michael addition, aldol-lactonization bicyclization, C-N bond formation and decarbonylation. Insights into these reactions can deepen the understanding of PKS-based assembly line chemistry and guide the efforts for rational engineering of polyketide-related molecules.

I 型多酮合成酶中酮合成酶结构域的非规范功能
模块化 I 型多酮合成酶(PKS)是一种非凡的分子机器,能够合成结构复杂的多酮天然产物,具有广泛的生物活性。在这些分子机器中,酮合成酶(KS)结构域发挥着核心作用,通常通过催化脱羧克莱森缩合作用来延长多酮链。越来越多具有催化功能而非克莱森缩合功能的非典型 KS 结构域被证实,这进一步证明了 I 型 PKS 结构多样性的能力。本综述概述了涉及不寻常 KS 活性的反应,包括 PKS 引物、酰基转移、迪克曼缩合、迈克尔加成、醛醇内酰化双环化、C-N 键形成和脱羰基化。对这些反应的深入了解可以加深对基于 PKS 的装配线化学的理解,并为聚酮相关分子的合理工程学研究提供指导。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
ChemBioChem
ChemBioChem 生物-生化与分子生物学
CiteScore
6.10
自引率
3.10%
发文量
407
审稿时长
1 months
期刊介绍: ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).
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