ArticleNature chemical biology2024
Biocatalytic cyclization of small macrolactams by a penicillin-binding protein-type thioesterase.
Article in Nature chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Discovery and Biosynthesis of the Novel Glycotetrapeptide Antibiotic Biffamycin A.Angewandte Chemie (International ed. in English) · 2026Article
- A Versatile Strategy for Head-to-Tail Macrocyclization and Traceless Backbone Editing of Short Peptides.Journal of the American Chemical Society · 2026Article
- Biocatalytic Tetrapeptide Macrocyclization by Cryptic Penicillin-Binding Protein-Type Thioesterases.Biochemistry · 2026Article
- Discovery and development of penicillin-binding protein-type thioesterases as biocatalysts.Current opinion in biotechnology · 2026Review
- Non-ribosomal peptide cyclase-directed chemoenzymatic synthesis of lariat lipopeptides.Nature chemistry · 2026Article
- Biocatalytic Tetrapeptide Macrocyclization by Cryptic Penicillin-binding Protein-type Thioesterases.bioRxiv : the preprint server for biology · 2025Article
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- Characterization of RufT Thioesterase Domain Reveals Insights into Rufomycin Cyclization and the Biosynthetic Origin of Rufomyazine.ACS chemical biology · 2025Article
- Synthetic-bioinformatic natural product-inspired peptides.Natural product reports · 2025Review
- Diol as a New Pantetheine Surrogate for Chemoenzymatic Synthesis of Cyclic Peptides via Nonribosomal Peptide Cyclases.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Macrocyclizing-thioesterases in bacterial non-ribosomal peptide biosynthesis.Journal of natural medicines · 2025Review
- Activity and Biocatalytic Potential of an Indolylamide Generating Thioesterase.Organic letters · 2024Article
- Advances, opportunities, and challenges in methods for interrogating the structure activity relationships of natural products.Natural product reports · 2024Review
- Chemoenzymatic tandem cyclization for the facile synthesis of bicyclic peptides.Communications chemistry · 2024Article
- Size matters.Nature chemical biology · 2024Article
- Chemo-enzymatic total synthesis: current approaches toward the integration of chemical and enzymatic transformations.Beilstein journal of organic chemistry · 2024Review
- Chemoenzymatic synthesis of macrocyclic peptides and polyketides via thioesterase-catalyzed macrocyclization.Beilstein journal of organic chemistry · 2024Review
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Authors and funding
8 authors.
Funding
Abstract
Macrocyclic peptides represent promising scaffolds for chemical tools and potential therapeutics. Synthetic methods for peptide macrocyclization are often hampered by C-terminal epimerization and oligomerization, leading to difficult scalability. While chemical strategies to circumvent this issue exist, they often require specific amino acids to be present in the peptide sequence. Herein, we report the characterization of Ulm16, a peptide cyclase belonging to the penicillin-binding protein-type class of thioesterases that catalyze head-to-tail macrolactamization of nonribosmal peptides. Ulm16 efficiently cyclizes various nonnative peptides ranging from 4 to 6 amino acids with catalytic efficiencies of up to 3 × 10
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