Details
| Original language | English |
|---|---|
| Pages (from-to) | 6372-6375 |
| Number of pages | 4 |
| Journal | Chemical communications |
| Volume | 57 |
| Issue number | 52 |
| Early online date | 24 May 2021 |
| Publication status | Published - 4 Jul 2021 |
| Externally published | Yes |
Abstract
Ribosomal natural products contain exquisite post-translational peptide modifications that are installed by a range of pathway-specific enzymes. We present proof of principle for a Sortase A-based approach that enables peptide modification by enzymes from unrelated pathways. This allowed the one-pot synthesis of a new-to-nature, hybrid ribosomal natural product.
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Materials Science(all)
- Electronic, Optical and Magnetic Materials
- Materials Science(all)
- Ceramics and Composites
- Chemistry(all)
- General Chemistry
- Materials Science(all)
- Surfaces, Coatings and Films
- Materials Science(all)
- Metals and Alloys
- Materials Science(all)
- Materials Chemistry
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In: Chemical communications, Vol. 57, No. 52, 04.07.2021, p. 6372-6375.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Leader peptide exchange to produce hybrid, new-to-nature ribosomal natural products
AU - Franz, Laura
AU - Koehnke, Jesko
N1 - Funding Information: We thank Dr Sebastian Adam for the expression and purification of MdnC. We thank the German Research Foundation for an Emmy Noether Fellowship (KO 4116/3-1) and the Boehringer Ingelheim Foundation (BIS) for an Exploration Grant.
PY - 2021/7/4
Y1 - 2021/7/4
N2 - Ribosomal natural products contain exquisite post-translational peptide modifications that are installed by a range of pathway-specific enzymes. We present proof of principle for a Sortase A-based approach that enables peptide modification by enzymes from unrelated pathways. This allowed the one-pot synthesis of a new-to-nature, hybrid ribosomal natural product.
AB - Ribosomal natural products contain exquisite post-translational peptide modifications that are installed by a range of pathway-specific enzymes. We present proof of principle for a Sortase A-based approach that enables peptide modification by enzymes from unrelated pathways. This allowed the one-pot synthesis of a new-to-nature, hybrid ribosomal natural product.
UR - http://www.scopus.com/inward/record.url?scp=85108879059&partnerID=8YFLogxK
U2 - 10.1039/d0cc06889f
DO - 10.1039/d0cc06889f
M3 - Article
C2 - 34075907
AN - SCOPUS:85108879059
VL - 57
SP - 6372
EP - 6375
JO - Chemical communications
JF - Chemical communications
SN - 1359-7345
IS - 52
ER -