ArticleNature chemical biology2009
Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes.
Article in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.
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Who cites it
116 citing papers in PubMed, 238 citations in OpenAlex.
- The tRNA moieties of both aminoacyl-tRNA substrates of a cyclodipeptide synthase share a common binding site, as revealed by RNA microhelices mimicking tRNA acceptor arms.Nucleic acids research · 2026Article
- Aminoacyl-tRNA-dependent enzymes in natural product biosynthesis: structure-function insights.The Journal of antibiotics · 2026Review
- A new-engineered integrative tool to target the terminal compartment of the Streptomyces chromosome.Applied microbiology and biotechnology · 2026Article
- Genomic insights into novelBurkholderia sp. Bmkn7 from coastal saline-affected rice fields unveils potential antimicrobial metabolites and plant growth-promoting traits.Scientific reports · 2026Article
- Genomic insights and evaluation ofFrontiers in cellular and infection microbiology · 2026Article
- Novel Antimicrobial Activities of Albofungin, Albonoursin, and Ribonucleosides Produced byMolecules (Basel, Switzerland) · 2025Article
- Article
- Biosynthesis of Unnatural Cyclodipeptides through Genetic Code Expansion and Cyclodipeptide Synthase Evolution.Journal of the American Chemical Society · 2025Article
- The iron chelator pulcherriminic acid mediates the light response in Bacillus subtilis biofilms.Nature communications · 2025Article
- Optimization of the Culture Conditions of Lactic Acid Bacteria for Antimicrobial Activity and Mass Production of Cyclic Dipeptides.Journal of microbiology and biotechnology · 2025Article
- Engineering a Biosynthetic Pathway to Produce (+)-Brevianamides A and B.ACS catalysis · 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
- Crystal Structure and Mutagenesis of an XYP Subfamily Cyclodipeptide Synthase Reveal Key Determinants of Enzyme Activity and Substrate Specificity.Biochemistry · 2024Article
- Exploring Sources, Biological Functions, and Potential Applications of the Ubiquitous Marine Cyclic Dipeptide: A Concise Review of Cyclic Glycine-Proline.Marine drugs · 2024Review
- Structure-Function Analysis of the EssentialInternational journal of molecular sciences · 2024Article
- Cyclodipeptide oxidase is an enzyme filament.Nature communications · 2024Article
- Heterologous pulcherrimin production in Saccharomyces cerevisiae confers inhibitory activity on Botrytis conidiation.FEMS yeast research · 2024Article
- Unveiling an indole alkaloid diketopiperazine biosynthetic pathway that features a unique stereoisomerase and multifunctional methyltransferase.Nature communications · 2023Article
- Genome mining for unknown-unknown natural products.Nature chemical biology · 2023Article
56 more citing papers are in PubMed but not listed here.
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Authors and funding
17 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyclodipeptides and their derivatives belong to the diketopiperazine (DKP) family, which is comprised of a broad array of natural products that exhibit useful biological properties. In the few known DKP biosynthetic pathways, nonribosomal peptide synthetases (NRPSs) are involved in the synthesis of cyclodipeptides that constitute the DKP scaffold, except in the albonoursin (1) pathway. Albonoursin, or cyclo(alpha,beta-dehydroPhe-alpha,beta-dehydroLeu), is an antibacterial DKP produced by Streptomyces noursei. In this pathway, the formation of the cyclo(Phe-Leu) (2) intermediate is catalyzed by AlbC, a small protein unrelated to NRPSs. We demonstrated that AlbC uses aminoacyl-tRNAs as substrates to catalyze the formation of the DKP peptide bonds. Moreover, several other bacterial proteins, presenting moderate similarity to AlbC, also use aminoacyl-tRNAs to synthesize various cyclodipeptides. Therefore, AlbC and these related proteins belong to a newly defined family of enzymes that we have named cyclodipeptide synthases (CDPSs).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.