ArticleApplied and environmental microbiology2009
Characterization of the complete zwittermicin A biosynthesis gene cluster from Bacillus cereus.
Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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64 citing papers in PubMed, 166 citations in OpenAlex.
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- Structure of a putative terminal amidation domain in natural product biosynthesis.Structure (London, England : 1993) · 2025Article
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- Microbiome composition modulates secondary metabolism in a multispecies bacterial community.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Comparison of Dinoflagellate Thiolation Domain Binding Proteins Using In Vitro and Molecular Methods.Marine drugs · 2022Article
- Dinoflagellate Phosphopantetheinyl Transferase (PPTase) and Thiolation Domain Interactions Characterized Using a Modified Indigoidine Synthesizing Reporter.Microorganisms · 2022Article
- Genome analysis of the salt-resistant Paludifilum halophilum DSM 102817World journal of microbiology & biotechnology · 2021Article
- Comparative genome analysis of Bacillus thuringiensis strain HD521 and HS18-1.Scientific reports · 2021Article
- Initiating polyketide biosynthesis by on-line methyl esterification.Nature communications · 2021Article
- Leveraging Microbial Genomes and Genomic Context for Chemical Discovery.Accounts of chemical research · 2021Article
- Discovery of Cyanobacterial Natural Products Containing Fatty Acid Residues*.Angewandte Chemie (International ed. in English) · 2021Article
- ThePathogens (Basel, Switzerland) · 2021Article
4 more citing papers are in PubMed but not listed here.
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3 authors at 2 institutions in 1 country.
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Abstract
Bacillus cereus UW85 produces the linear aminopolyol antibiotic zwittermicin A (ZmA). This antibiotic has diverse biological activities, such as suppression of disease in plants caused by protists, inhibition of fungal and bacterial growth, and amplification of the insecticidal activity of the toxin protein from Bacillus thuringiensis. ZmA has an unusual chemical structure that includes a d amino acid and ethanolamine and glycolyl moieties, as well as having an unusual terminal amide that is generated from the modification of the nonproteinogenic amino acid beta-ureidoalanine. The diverse biological activities and unusual structure of ZmA have stimulated our efforts to understand how this antibiotic is biosynthesized. Here, we present the identification of the complete ZmA biosynthesis gene cluster from B. cereus UW85. A nearly identical gene cluster is identified on a plasmid from B. cereus AH1134, and we show that this strain is also capable of producing ZmA. Bioinformatics and biochemical analyses of the ZmA biosynthesis enzymes strongly suggest that ZmA is initially biosynthesized as part of a larger metabolite that is processed twice, resulting in the formation of ZmA and two additional metabolites. Additionally, we propose that the biosynthesis gene cluster for the production of the amino sugar kanosamine is contained within the ZmA biosynthesis gene cluster in B. cereus UW85.
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