ArticleNature communications2024
Cyclodipeptide oxidase is an enzyme filament.
Article in Nature communications, 2024. 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, 10 citations in OpenAlex.
- Novel Antimicrobial Activities of Albofungin, Albonoursin, and Ribonucleosides Produced byMolecules (Basel, Switzerland) · 2025Article
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- Engineering a Biosynthetic Pathway to Produce (+)-Brevianamides A and B.ACS catalysis · 2025Article
- In Vitro and In Silico Studies of Maculosin as a Melanogenesis and Tyrosinase Inhibitor.Molecules (Basel, Switzerland) · 2025Article
- Broad substrate scope C-C oxidation in cyclodipeptides catalysed by a flavin-dependent filament.Nature communications · 2025Article
- Genome mining of albocandins A-E fromRSC advances · 2025Article
- The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell.Nature communications · 2024Article
- The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell.bioRxiv : the preprint server for biology · 2024Article
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2 authors at 1 institution in 1 country.
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Abstract
Modified cyclic dipeptides represent a widespread class of secondary metabolites with diverse pharmacological activities, including antibacterial, antifungal, and antitumor. Here, we report the structural characterization of the Streptomyces noursei enzyme AlbAB, a cyclodipeptide oxidase (CDO) carrying out α,β-dehydrogenations during the biosynthesis of the antibiotic albonoursin. We show that AlbAB is a megadalton heterooligomeric enzyme filament containing covalently bound flavin mononucleotide cofactors. We highlight that AlbAB filaments consist of alternating dimers of AlbA and AlbB and that enzyme activity is crucially dependent on filament formation. We show that AlbA-AlbB interactions are highly conserved suggesting that other CDO-like enzymes are likely enzyme filaments. As CDOs have been employed in the structural diversification of cyclic dipeptides, our results will be useful for future applications of CDOs in biocatalysis and chemoenzymatic synthesis.
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