ArticleJournal of the American Chemical Society2015
Understanding Programming of Fungal Iterative Polyketide Synthases: The Biochemical Basis for Regioselectivity by the Methyltransferase Domain in the Lovastatin Megasynthase.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 93 citations in OpenAlex.
- Stereochemical Dissection of the Strobilurin PKS Reveals the Complex Biosynthetic Logic of Iterative EZE Triene Construction.Angewandte Chemie (International ed. in English) · 2026Article
- Substrate specificities of two ketosynthases in eukaryotic microalgal and prokaryotic marine bacterial DHA synthases.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Biosynthesis of the Antifungal Polyhydroxy-Polyketide Acrophialocinol.Organic letters · 2025Article
- Fungal BGCs for Production of Secondary Metabolites: Main Types, Central Roles in Strain Improvement, and Regulation According to the Piano Principle.International journal of molecular sciences · 2023Review
- A genetic tool to express long fungal biosynthetic genes.Fungal biology and biotechnology · 2023Article
- Deciphering chemical logic of fungal natural product biosynthesis through heterologous expression and genome mining.Natural product reports · 2023Review
- Domain Truncation in Hispidin Synthase Orthologs from Non-Bioluminescent Fungi Does Not Lead to Hispidin Biosynthesis.International journal of molecular sciences · 2023Article
- Functional analysis of the dehydratase domains of the PUFA synthase from Emiliania huxleyi in Escherichia coli and Arabidopsis thaliana.Biotechnology for biofuels and bioproducts · 2022Article
- Secondary metabolites from hypocrealean entomopathogenic fungi: novel bioactive compounds.Natural product reports · 2020Review
- Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase.RSC advances · 2020Article
- Molecular basis of methylation and chain-length programming in a fungal iterative highly reducing polyketide synthase.Chemical science · 2019Article
- Genome mining and biosynthesis of a polyketide from a biofertilizer fungus that can facilitate reductive iron assimilation in plant.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Crystal structure of the condensation domain from lovastatin polyketide synthase.Synthetic and systems biotechnology · 2019Article
- Biochemical characterization of the minimal domains of an iterative eukaryotic polyketide synthase.The FEBS journal · 2018Article
- 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
- Biosynthesis of Long-Chain N-Acyl Amide by a Truncated Polyketide Synthase-Nonribosomal Peptide Synthetase Hybrid Megasynthase in Fungi.Journal of the American Chemical Society · 2018Article
- Article
- Reversible Product Release and Recapture by a Fungal Polyketide Synthase Using a Carnitine Acyltransferase Domain.Angewandte Chemie (International ed. in English) · 2017Article
- A scalable platform to identify fungal secondary metabolites and their gene clusters.Nature chemical biology · 2017Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Highly reducing polyketide synthases (HR-PKSs) from fungi synthesize complex natural products using a single set of domains in a highly programmed, iterative fashion. The most enigmatic feature of HR-PKSs is how tailoring domains function selectively during different iterations of chain elongation to afford structural diversity. Using the lovastatin nonaketide synthase LovB as a model system and a variety of acyl substrates, we characterized the substrate specificity of the LovB methyltransferase (MT) domain. We showed that, while the MT domain displays methylation activity toward different β-ketoacyl groups, it is exceptionally selective toward its naturally programmed β-keto-dienyltetraketide substrate with respect to both chain length and functionalization. Accompanying characterization of the ketoreductase (KR) domain displays broader substrate specificity toward different β-ketoacyl groups. Our studies indicate that selective modifications by tailoring domains, such as the MTs, are achieved by higher kinetic efficiency on a particular substrate relative to the rate of transformation by other competing domains.
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