ArticleACS synthetic biology2013
Sequence, cloning, and analysis of the fluvirucin B1 polyketide synthase from Actinomadura vulgaris.
Article in ACS synthetic biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Substrate Trapping in Polyketide Synthase Thioesterase Domains: Structural Basis for Macrolactone Formation.ACS catalysis · 2024Article
- Chemistry and biology of specialized metabolites produced byNatural product reports · 2024Review
- Fluvirucins BRSC advances · 2022Article
- Biosynthetic Cyclization Catalysts for the Assembly of Peptide and Polyketide Natural Products.ChemCatChem · 2021Article
- Food-Poisoning Bacteria Employ a Citrate Synthase and a Type II NRPS To Synthesize Bolaamphiphilic Lipopeptide Antibiotics*.Angewandte Chemie (International ed. in English) · 2020Article
- Structural insights into dehydratase substrate selection for the borrelidin and fluvirucin polyketide synthases.Journal of industrial microbiology & biotechnology · 2019Article
- Fluvirucin B6, a new macrolactam isolated from a marine-derived actinomycete of the genus Nocardiopsis.The Journal of antibiotics · 2018Article
- Anti-trypanosomal compound, sagamilactam, a new polyene macrocyclic lactam from Actinomadura sp. K13-0306.The Journal of antibiotics · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Fluvirucin B1 , produced by Actinomadura vulgaris, is a 14-membered macrolactam active against a variety of infectious fungi as well as influenza A. Despite considerable interest from the synthetic community, very little information is available regarding the biosynthetic origins of the fluvirucins. Herein, we report the identification and initial characterization of the fluvirucin B1 polyketide synthase and related enzymes. The cluster consists of five extender modules flanked by an N-terminal acyl carrier protein and C-terminal thioesterase domain. All but one of the synthase modules contain the full complement of tailoring domains (ketoreductase, dehydratase, and enoyl reductase) as determined by sequence homology with known polyketide synthases. Acitve site analyses of several key components of the cluster are performed to further verify that this gene cluster is associated with production of fluvirucin B1 . This work will both open doors toward a better understanding of macrolactam formation and provide an avenue to genetics-based diversification of fluvirucin structure.
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Registered trials
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