ArticleProceedings of the National Academy of Sciences of the United States of America2006
Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 177 citations in OpenAlex.
- Extending the starter-unit selection of a collaborating non-reducing polyketide synthase through rational domain swaps.RSC advances · 2026Article
- Engineering a Fungal Non-Reducing Polyketide Synthase with an Apparently Inactive Product-Template Domain Reveals Insights into the Catalytic Reprogramming.International journal of molecular sciences · 2026Article
- A hybrid assembly mechanism employs nonreducing polyketide synthase-like logic for partially reduced polyketide formation.Marine life science & technology · 2026Article
- Biosynthesis of the Paecilomyces marquandii conidial pigment saintopin.Fungal biology and biotechnology · 2025Article
- Article
- Combinatorial biosynthesis for the engineering of novel fungal natural products.Communications chemistry · 2024Review
- Biosynthesis of Cytosporones in Leotiomycetous Filamentous Fungi.Journal of the American Chemical Society · 2024Article
- Basidiomycete non-reducing polyketide synthases function independently of SAT domains.Fungal biology and biotechnology · 2023Article
- The 'emodin family' of fungal natural products-amalgamating a century of research with recent genomics-based advances.Natural product reports · 2023Review
- Deciphering chemical logic of fungal natural product biosynthesis through heterologous expression and genome mining.Natural product reports · 2023Review
- Linking Lichen Metabolites to Genes: Emerging Concepts and Lessons from Molecular Biology and Metagenomics.Journal of fungi (Basel, Switzerland) · 2023Review
- Unprecedented Mushroom Polyketide Synthases Produce the Universal Anthraquinone Precursor.Angewandte Chemie (International ed. in English) · 2022Article
- Subcellular localization of fungal specialized metabolites.Fungal biology and biotechnology · 2022Review
- Synthaser: a CD-Search enabled Python toolkit for analysing domain architecture of fungal secondary metabolite megasynth(et)ases.Fungal biology and biotechnology · 2021Article
- High-Titer Production of Olivetolic Acid and Analogs in Engineered Fungal Host Using a Nonplant Biosynthetic Pathway.ACS synthetic biology · 2021Article
- Biosynthesis of 6-Hydroxymellein Requires a Collaborating Polyketide Synthase-like Enzyme.Angewandte Chemie (International ed. in English) · 2021Article
- Intrinsic and Extrinsic Programming of Product Chain Length and Release Mode in Fungal Collaborating Iterative Polyketide Synthases.Journal of the American Chemical Society · 2020Article
- Characteristics, Occurrence, Detection and Detoxification of Aflatoxins in Foods and Feeds.Foods (Basel, Switzerland) · 2020Review
- The role of the iterative modules in polyketide synthase evolution.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Chimeric 6-methylsalicylic acid synthase with domains of acyl carrier protein and methyltransferase from Pseudallescheria boydii shows novel biosynthetic activity.Microbial biotechnology · 2019Article
24 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Polyketides are a class of natural products that exhibit a wide range of functional and structural diversity. They include antibiotics, immunosuppressants, antifungals, antihypercholesterolemics, and cytotoxins. Polyketide synthases (PKSs) use chemistry similar to fatty acid synthases (FASs), although building block variation and differing extents of reduction of the growing polyketide chain underlie their biosynthetic versatility. In contrast to the well studied sequential modular type I PKSs, less is known about how the iterative type I PKSs carry out and control chain initiation, elongation, folding, and cyclization during polyketide processing. Domain structure analysis of a group of related fungal, nonreducing PKSs has revealed well defined N-terminal domains longer than commonly seen for FASs and modular PKSs. Predicted structure of this domain disclosed a region similar to malonyl-CoA:acyl-carrier protein (ACP) transacylases (MATs). MATs play a key role transferring precursor CoA thioesters from solution onto FASs and PKSs for chain elongation. On the basis of site-directed mutagenesis, radiolabeling, and kinetics experiments carried out with individual domains of the norsolorinic acid PKS, we propose that the N-terminal domain is a starter unit:ACP transacylase (SAT domain) that selects a C(6) fatty acid from a dedicated yeast-like FAS and transfers this unit onto the PKS ACP, leading to the production of the aflatoxin precursor, norsolorinic acid. These findings could indicate a much broader role for SAT domains in starter unit selection among nonreducing iterative, fungal PKSs, and they provide a biochemical rationale for the classical acetyl "starter unit effect."
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.