ArticleNature communications2020
Minimal lactazole scaffold for in vitro thiopeptide bioengineering.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- De Novo Discovery of Nonstandard Thioisoindole-Bridged Bicyclic Peptides Targeting Traf2- and NCK-Interacting Kinase.Angewandte Chemie (International ed. in English) · 2026Article
- P450 cyptide synthase KwwB catalyzes non-native cross-link at Tyr-C3-Trp-N1 and tolerates leader peptide mutations.The Journal of antibiotics · 2026Article
- A Framework for the In Vivo Production of Extensively Engineered Thiopeptides.ACS synthetic biology · 2026Article
- Protocol for in vitro chemoenzymatic synthesis of thiazole-containing macrocyclic peptides via ribosomal incorporation of thioamides.STAR protocols · 2026Article
- mRNA Display for Identifying Peptide Substrates of Enzymes.Biochemistry · 2026Review
- Ribosomal Synthesis of Topologically Defined Thioisoindole-Bridged Bicyclic Peptides.Angewandte Chemie (International ed. in English) · 2026Article
- P450 Cyptide Synthase KwwB Catalyzes Trp-C5-Trp-N1 Cross-Linking and Accepts Diverse Precursor Peptides.Organic letters · 2026Article
- Assessing Substrate Scope of the Cyclodehydratase LynD by mRNA Display-Enabled Machine Learning Models.Biochemistry · 2025Article
- Unlocking hidden bioactive compounds: from indolocarbazole and RiPP biosynthesis to the activation of cryptic secondary metabolism via microbial interactions.The Journal of antibiotics · 2025Review
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- Substrate recognition by a peptide-aminoacyl-tRNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Ligand-Enabled Selective Coupling of MIDA Boronates to Dehydroalanine-Containing Peptides and Proteins.Journal of the American Chemical Society · 2025Article
- Substrate prediction for RiPP biosynthetic enzymesDigital discovery · 2025Article
- De novo design of ribosomally synthesized and post-translationally modified peptides.Nature chemistry · 2025Article
- RiPP Enzymes for Biosynthetically Derived Cyclic Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2025Review
- Kinetic Analysis of Cyclization by the Substrate-Tolerant Lanthipeptide Synthetase ProcM.ACS catalysis · 2024Article
- Embleporicin: A Novel Class I Lanthipeptide from the ActinobacteriaAntibiotics (Basel, Switzerland) · 2024Article
- Cell-Free Systems: Ideal Platforms for Accelerating the Discovery and Production of Peptide-Based Antibiotics.International journal of molecular sciences · 2024Review
- Expression and Subcellular Localization of Lanthipeptides in Human Cells.ACS synthetic biology · 2024Article
- Employing unnatural promiscuity of sortase to construct peptide macrocycle libraries for ligand discovery.Chemical science · 2024Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactazole A is a cryptic thiopeptide from Streptomyces lactacystinaeus, encoded by a compact 9.8 kb biosynthetic gene cluster. Here, we establish a platform for in vitro biosynthesis of lactazole A, referred to as the FIT-Laz system, via a combination of the flexible in vitro translation (FIT) system with recombinantly produced lactazole biosynthetic enzymes. Systematic dissection of lactazole biosynthesis reveals remarkable substrate tolerance of the biosynthetic enzymes and leads to the development of the minimal lactazole scaffold, a construct requiring only 6 post-translational modifications for macrocyclization. Efficient assembly of such minimal thiopeptides with FIT-Laz opens access to diverse lactazole analogs with 10 consecutive mutations, 14- to 62-membered macrocycles, and 18 amino acid-long tail regions, as well as to hybrid thiopeptides containing non-proteinogenic amino acids. This work suggests that the minimal lactazole scaffold is amenable to extensive bioengineering and opens possibilities to explore untapped chemical space of thiopeptides.
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