ArticleProceedings of the National Academy of Sciences of the United States of America2012
Crystal structure and biochemical studies of the trans-acting polyketide enoyl reductase LovC from lovastatin biosynthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. 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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Who cites it
31 citing papers in PubMed, 94 citations in OpenAlex.
- Black yeasts are efficient heterologous hosts for the production of a wide range of fungal polyketides.Nature chemical biology · 2026Article
- High-Throughput Prediction of Protein-Protein Interactions Uncovers Hidden Molecular Networks in Biosynthetic Gene Clusters.Computational and structural biotechnology journal · 2026Article
- The Role of Enoyl Reductase in the Monacolin K Biosynthesis Pathway inJournal of fungi (Basel, Switzerland) · 2025Article
- Non-ribosomal peptide synthetase (NRPS)-encoding products and their biosynthetic logics in Fusarium.Microbial cell factories · 2024Review
- Antibiotic Skeletal Diversification via Differential Enoylreductase Recruitment and Module Iteration inJournal of the American Chemical Society · 2024Article
- 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
- Biosynthesis of the Isocoumarin Derivatives Fusamarins is Mediated by the PKS8 Gene Cluster in Fusarium.Chembiochem : a European journal of chemical biology · 2023Article
- Recent advances in the chemo-biological characterization of decalin natural products and unraveling of the workings of Diels-Alderases.Fungal biology and biotechnology · 2022Review
- Heterologous Synthesis of Monacolin J by Reconstructing Its Biosynthetic Gene Cluster inJournal of fungi (Basel, Switzerland) · 2022Article
- Kupyaphores are zinc homeostatic metallophores required for colonization ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Saccharomyces cerevisiae as host for the recombinant production of polyketides and nonribosomal peptides.Microbial cell factories · 2021Review
- Biosynthesis of 6-Hydroxymellein Requires a Collaborating Polyketide Synthase-like Enzyme.Angewandte Chemie (International ed. in English) · 2021Article
- Structural basis for the biosynthesis of lovastatin.Nature communications · 2021Article
- 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
- Engineering actinomycetes for biosynthesis of macrolactone polyketides.Microbial cell factories · 2019Review
- A comprehensive catalogue of polyketide synthase gene clusters in lichenizing fungi.Journal of industrial microbiology & biotechnology · 2018Review
- The architectures of iterative type I PKS and FAS.Natural product reports · 2018Review
- A conserved threonine prevents self-intoxication of enoyl-thioester reductases.Nature chemical biology · 2017Article
- An Iterative Module in the Azalomycin F Polyketide Synthase Contains a Switchable Enoylreductase Domain.Angewandte Chemie (International ed. in English) · 2017Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
Lovastatin is an important statin prescribed for the treatment and prevention of cardiovascular diseases. Biosynthesis of lovastatin uses an iterative type I polyketide synthase (PKS). LovC is a trans-acting enoyl reductase (ER) that specifically reduces three out of eight possible polyketide intermediates during lovastatin biosynthesis. Such trans-acting ERs have been reported across a variety of other fungal PKS enzymes as a strategy in nature to diversify polyketides. How LovC achieves such specificity is unknown. The 1.9-Å structure of LovC reveals that LovC possesses a medium-chain dehydrogenase/reductase (MDR) fold with a unique monomeric assembly. Two LovC cocrystal structures and enzymological studies help elucidate the molecular basis of LovC specificity, define stereochemistry, and identify active-site residues. Sequence alignment indicates a general applicability to trans-acting ERs of fungal PKSs, as well as their potential application to directing biosynthesis.
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