ArticleJournal of industrial microbiology & biotechnology2021
PenA, a penicillin-binding protein-type thioesterase specialized for small peptide cyclization.
Article in Journal of industrial microbiology & biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- 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
- 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
- Macrocyclizing-thioesterases in bacterial non-ribosomal peptide biosynthesis.Journal of natural medicines · 2025Review
- Chemoenzymatic tandem cyclization for the facile synthesis of bicyclic peptides.Communications chemistry · 2024Article
- Size matters.Nature chemical biology · 2024Article
- Biocatalytic cyclization of small macrolactams by a penicillin-binding protein-type thioesterase.Nature chemical biology · 2024Article
- Chemo-Enzymatic Synthesis of Non-ribosomal Macrolactams by a Penicillin-Binding Protein-Type Thioesterase.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Introduction to the special issue: "Natural Product Discovery and Development in the Genomic Era: 2021".Journal of industrial microbiology & biotechnology · 2021Article
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Authors and funding
3 authors.
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Abstract
Penicillin-binding protein-type thioesterases (PBP-type TEs) are a recently identified group of peptide cyclases that catalyze head-to-tail macrolactamization of nonribosomal peptides. PenA, a new member of this group, is involved in the biosyntheses of cyclic pentapeptides. In this study, we demonstrated the enzymatic activity of PenA in vitro, and analyzed its substrate scope with a series of synthetic substrates. A comparison of the reaction profiles between PenA and SurE, a representative PBP-type TE, showed that PenA is more specialized for small peptide cyclization. A computational model provided a possible structural rationale for the altered specificity for substrate chain lengths.
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