ArticleNature chemical biology2016
Amino-group carrier-protein-mediated secondary metabolite biosynthesis in Streptomyces.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 37 citations in OpenAlex.
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- Orthogonal Biosynthesis of Pyrrolamides through Dehydration by a Pathway-Specific Glycoside Hydrolase-Like Enzyme in Gram-Positive Bacteria.Journal of the American Chemical Society · 2026Article
- Biomimetic Total Synthesis and Paired Omics Identify an Intermolecular Diels-Alder Reaction as the Key Step in Lugdunomycin Biosynthesis.Journal of the American Chemical Society · 2025Article
- Identification of four novelInternational journal of systematic and evolutionary microbiology · 2025Article
- Crystal structure of a novel heterooligomeric aminotransferase from Serratia sp. ATCC 39006 provides insights into function.FEBS letters · 2025Article
- Distribution, abundance, and ecogenomics of themSystems · 2023Article
- Discovery and biosynthetic assessment of 'Microbial genomics · 2023Article
- Biosynthesis of DNA-Alkylating Antitumor Natural Products.Molecules (Basel, Switzerland) · 2022Review
- Biosynthesis of 3-thia-α-amino acids on a carrier peptide.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Substrate Recognition by the Peptidyl-(ACS chemical biology · 2022Article
- Use of a scaffold peptide in the biosynthesis of amino acid-derived natural products.Science (New York, N.Y.) · 2019Article
- Refining and expanding nonribosomal peptide synthetase function and mechanism.Journal of industrial microbiology & biotechnology · 2019Review
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Authors and funding
13 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Amino-group carrier proteins (AmCPs) mediate the biosynthesis of lysine and arginine in some bacteria and archaea. Here we demonstrate that an uncharacterized AmCP-mediated biosynthetic system functions to biosynthesize the previously uncharacterized and nonproteinogenic amino acid (2S,6R)-diamino-(5R,7)-dihydroxy-heptanoic acid (DADH) in Streptomyces sp. SANK 60404. DADH is incorporated into a novel peptide metabolite, vazabitide A, featuring an azabicyclo-ring structure, by nonribosomal peptide synthetases and successive modification enzymes in this bacterium. As the AmCP-mediated machinery for DADH biosynthesis is widely distributed in bacteria, further analysis of uncharacterized AmCP-containing gene clusters will lead to the discovery of novel bioactive compounds and novel biosynthetic enzymes.
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