ArticleACS chemical biology2019
Engineering of Chimeric Polyketide Synthases Using SYNZIP Docking Domains.
Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Evolutionary Reprogramming of Acyltransferase Domains in Polyene Macrolide Pathways.Microorganisms · 2026Article
- Plug-and-play engineering of modular polyketide synthases.Nature chemical biology · 2025Article
- Design principles imprinted by evolution.Nature chemical biology · 2025Article
- Docking domains from modular polyketide synthases and their use in engineering.Nature communications · 2025Article
- Guidelines for Optimizing Type S Nonribosomal Peptide Synthetases.ACS synthetic biology · 2023Article
- Integration of multiple stress signals in plants using synthetic Boolean logic gates.Plant physiology · 2023Article
- Enzymology of assembly line synthesis by modular polyketide synthases.Nature chemical biology · 2023Review
- Microbial synthesis of long-chain α-alkenes from methanol by engineering Pichia pastoris.Bioresources and bioprocessing · 2022Article
- Type S Non-Ribosomal Peptide Synthetases for the Rapid Generation of Tailormade Peptide Libraries.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Article
- Synthetic Zippers as an Enabling Tool for Engineering of Non-Ribosomal Peptide Synthetases*.Angewandte Chemie (International ed. in English) · 2021Article
- Docking domain-mediated subunit interactions in natural product megasynth(et)ases.Journal of industrial microbiology & biotechnology · 2021Review
- Synthetic biology enabling access to designer polyketides.Current opinion in chemical biology · 2020Review
- Interfacial plasticity facilitates high reaction rate ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Repurposing Modular Polyketide Synthases and Non-ribosomal Peptide Synthetases for Novel Chemical Biosynthesis.Frontiers in molecular biosciences · 2020Review
- Evolution and Diversity of Assembly-Line Polyketide Synthases.Chemical reviews · 2019Review
- Probing the structure and function of acyl carrier proteins to unlock the strategic redesign of type II polyketide biosynthetic pathways.The Journal of biological chemistryReview
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Authors and funding
5 authors.
Funding
Abstract
Engineering of assembly line polyketide synthases (PKSs) to produce novel bioactive compounds has been a goal for over 20 years. The apparent modularity of PKSs has inspired many engineering attempts in which entire modules or single domains were exchanged. In recent years, it has become evident that certain domain-domain interactions are evolutionarily optimized and, if disrupted, cause a decrease of the overall turnover rate of the chimeric PKS. In this study, we compared different types of chimeric PKSs in order to define the least invasive interface and to expand the toolbox for PKS engineering. We generated bimodular chimeric PKSs in which entire modules were exchanged, while either retaining a covalent linker between heterologous modules or introducing a noncovalent docking domain, or SYNZIP domain, mediated interface. These chimeric systems exhibited non-native domain-domain interactions during intermodular polyketide chain translocation. They were compared to otherwise equivalent bimodular PKSs in which a noncovalent interface was introduced between the condensing and processing parts of a module, resulting in non-native domain interactions during the extender unit acylation and polyketide chain elongation steps of their catalytic cycles. We show that the natural PKS docking domains can be efficiently substituted with SYNZIP domains and that the newly introduced noncovalent interface between the condensing and processing parts of a module can be harnessed for PKS engineering. Additionally, we established SYNZIP domains as a new tool for engineering PKSs by efficiently bridging non-native interfaces without perturbing PKS activity.
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