ArticleNature communications2021
Efficient biosynthesis of nucleoside cytokinin angustmycin A containing an unusual sugar system.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Biosynthesis of Benzohydroxamic Acid inJournal of natural products · 2026Article
- New insights into the microbiome of the deep-sea spongeMicrobial genomics · 2026Article
- A combined pseudouridine biomanufacturing platform enabled by a streamlined designer pathway.Nature communications · 2025Article
- Direct and efficient synthesis of nucleosides through the ortho-(tert-butylethynyl)phenyl thioglycosides (BEPTs) protocol.Nature communications · 2025Article
- ScnR1-Mediated Competitive DNA Binding and Feedback Inhibition Regulate Guvermectin Biosynthesis inBiology · 2025Article
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- Biosynthesis and genome mining strategies for purine-derivedFrontiers in microbiology · 2025Review
- Coordinated regulation of two LacI family regulators, GvmR and GvmR2, on guvermectin production inSynthetic and systems biotechnology · 2025Article
- Phylogenomics of novel clones ofMicrobiology spectrum · 2024Article
- Purine nucleoside antibiotics: recent synthetic advances harnessing chemistry and biology.Natural product reports · 2024Review
- Biology of Two-Spotted Spider Mite (International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Angustmycin A has anti-mycobacterial and cytokinin activities, and contains an intriguing structure in which an unusual sugar with C5'-C6' dehydration is linked to adenine via an N-glycosidic bond. However, the logic underlying the biosynthesis of this molecule has long remained obscure. Here, we address angustmycin A biosynthesis by the full deciphering of its pathway. We demonstrate that AgmD, C, A, E, and B function as D-allulose 6-phosphate 3-epimerase, D-allulose 6-phosphate pyrophosphokinase, adenine phosphoallulosyltransferase, phosphoribohydrolase, and phosphatase, respectively, and that these collaboratively catalyze the relay reactions to biosynthesize angustmycin C. Additionally, we provide evidence that AgmF is a noncanonical dehydratase for the final step to angustmycin A via a self-sufficient strategy for cofactor recycling. Finally, we have reconstituted the entire six-enzyme pathway in vitro and in E. coli leading to angustmycin A production. These results expand the enzymatic repertoire regarding natural product biosynthesis, and also open the way for rational and rapid discovery of other angustmycin related antibiotics.
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