Abstract
The conserved threonine (Thr) residue in the penultimate position of the leader peptide of lasso peptides microcin J25 and capistruin can be effectively replaced by several amino acids close in size and shape to Thr. These findings suggest a model for lasso peptide biosynthesis in which the Thr sidechain is a recognition element for the lasso peptide maturation machinery.
Original language | English (US) |
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Pages (from-to) | 1880-1882 |
Number of pages | 3 |
Journal | Chemical Communications |
Volume | 48 |
Issue number | 13 |
DOIs | |
State | Published - Jan 16 2012 |
All Science Journal Classification (ASJC) codes
- Electronic, Optical and Magnetic Materials
- General Chemistry
- Ceramics and Composites
- Metals and Alloys
- Materials Chemistry
- Surfaces, Coatings and Films
- Catalysis