ArticleACS chemical biology2015
Starter unit flexibility for engineered product synthesis by the nonreducing polyketide synthase PksA.
Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 36 citations in OpenAlex.
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- Combinatorial biosynthesis for the engineering of novel fungal natural products.Communications chemistry · 2024Review
- Biosynthetic gene cluster synteny: Orthologous polyketide synthases in Hypogymnia physodes, Hypogymnia tubulosa, and Parmelia sulcata.MicrobiologyOpen · 2023Article
- Biosynthetic Potential ofJournal of fungi (Basel, Switzerland) · 2023Article
- The Ketosynthase Domain Controls Chain Length in Mushroom Oligocyclic Polyketide Synthases.Chembiochem : a European journal of chemical biology · 2023Article
- Article
- Intrinsic and Extrinsic Programming of Product Chain Length and Release Mode in Fungal Collaborating Iterative Polyketide Synthases.Journal of the American Chemical Society · 2020Article
- Exploring Fungal Polyketide C-Methylation through Combinatorial Domain Swaps.ACS chemical biology · 2018Article
- The architectures of iterative type I PKS and FAS.Natural product reports · 2018Review
- Saccharomonopyrones A-C, New α-Pyrones from a Marine Sediment-Derived Bacterium Saccharomonospora sp. CNQ-490.Marine drugs · 2017Article
- Functional and Structural Analysis of Programmed C-Methylation in the Biosynthesis of the Fungal Polyketide Citrinin.Cell chemical biology · 2017Article
- Insight into different environmental niches adaptation and allergenicity from the Cladosporium sphaerospermum genome, a common human allergy-eliciting Dothideomycetes.Scientific reports · 2016Article
- Diversity-Oriented Combinatorial Biosynthesis of Hybrid Polyketide Scaffolds from Azaphilone and Benzenediol Lactone Biosynthons.Organic letters · 2016Article
- Harnessing natural product assembly lines: structure, promiscuity, and engineering.Journal of industrial microbiology & biotechnology · 2016Review
- Insights into 6-Methylsalicylic Acid Bio-assembly by Using Chemical Probes.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2016Article
- Insights into 6-Methylsalicylic Acid Bio-assembly by Using Chemical Probes.Angewandte Chemie (International ed. in English) · 2016Article
- Recent Advances in Understanding and Engineering Polyketide Synthesis.F1000Research · 2016Review
- Biochemical and Structural Basis for Controlling Chemical Modularity in Fungal Polyketide Biosynthesis.Journal of the American Chemical Society · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Nonreducing polyketide synthases (NR-PKSs) are unique among PKSs in their domain structure, notably including a starter unit:acyl-carrier protein (ACP) transacylase (SAT) domain that selects an acyl group as the primer for biosynthesis, most commonly acetyl-CoA from central metabolism. This clan of mega-enzymes resembles fatty acid synthases (FASs) by sharing both their central chain elongation steps and their capacity for iterative catalysis. In this mode of synthesis, catalytic domains involved in chain extension exhibit substrate plasticity to accommodate growing chains as small as two carbons to 20 or more. PksA is the NR-PKS central to the biosynthesis of the mycotoxin aflatoxin B1 whose SAT domain accepts an unusual hexanoyl starter from a dedicated yeast-like FAS. Explored in this paper is the ability of PksA to utilize a selection of potential starter units as substrates to initiate and sustain extension and cyclization to on-target, programmed polyketide synthesis. Most of these starter units were successfully accepted and properly processed by PksA to achieve biosynthesis of the predicted naphthopyrone product. Analysis of the on-target and derailment products revealed trends of tolerance by individual PksA domains to alternative starter units. In addition, natural and un-natural variants of the active site cysteine were examined and found to be capable of biosynthesis, suggesting possible direct loading of starter units onto the β-ketoacyl synthase (KS) domain. In light of the data assembled here, the predictable synthesis of unnatural products by NR-PKSs is more fully defined.
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