ArticleRSC chemical biology2022
Developing crosslinkers specific for epimerization domain in NRPS initiation modules to evaluate mechanism.
Article in RSC chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Total Synthesis and Structural Revision of Rhabdobranin Reveals a Cryptic Gram-Negative Antibiotic.Journal of the American Chemical Society · 2026Article
- The Potential of Non-Ribosomal Peptide Engineering for Creating New Antimicrobial Complexes.Molecules (Basel, Switzerland) · 2026Review
- Article
- Genomic Comparison of Two Species ofJournal of fungi (Basel, Switzerland) · 2023Article
- Recent Advances in Cyanotoxin Synthesis and Applications: A Comprehensive Review.Microorganisms · 2023Review
- Structure modification of an antibiotic: by engineering the fusaricidin bio-synthetase A inFrontiers in microbiology · 2023Article
- Translocation of subunit PPSE in plipastatin synthase and synthesis of novel lipopeptides.Synthetic and systems biotechnology · 2022Article
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Authors and funding
8 authors.
Funding
Abstract
Nonribosomal peptide synthetases (NRPSs) are complex multi-modular enzymes containing catalytic domains responsible for the loading and incorporation of amino acids into natural products. These unique molecular factories can produce peptides with nonproteinogenic d-amino acids in which the epimerization (E) domain catalyzes the conversion of l-amino acids to d-amino acids, but its mechanism remains not fully understood. Here, we describe the development of pantetheine crosslinking probes that mimic the natural substrate l-Phe of the initiation module of tyrocidine synthetase, TycA, to elucidate and study the catalytic residues of the E domain. Mechanism-based crosslinking assays and MALDI-TOF MS were used to identify both H743 and E882 as the crosslinking site residues, demonstrating their roles as catalytic bases. Mutagenesis studies further validated these results and allowed the comparison of reactivity between the catalytic residues, concluding that glutamate acts as the dominant nucleophile in the crosslinking reaction, resembling the deprotonation of the C
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Registered trials
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