Nonribosomal Peptide Biosynthesis: Point Mutations and Module Skipping Lead to Chemical Diversity

2006 ◽  
Vol 45 (14) ◽  
pp. 2296-2301 ◽  
Author(s):  
Silke C. Wenzel ◽  
Peter Meiser ◽  
Tina M. Binz ◽  
Taifo Mahmud ◽  
Rolf Müller
Keyword(s):  
Point Mutations ◽  
Chemical Diversity ◽  
Nonribosomal Peptide ◽  
Peptide Biosynthesis

scholarly journals Rational Design of a Bimodular Model System for the Investigation of Heterocyclization in Nonribosomal Peptide Biosynthesis

2004 ◽  
Vol 11 (2) ◽  
pp. 261-271 ◽  
Author(s):  
Thomas Duerfahrt ◽  
Katrin Eppelmann ◽  
Rolf Müller ◽  
Mohamed A. Marahiel
Keyword(s):  
Rational Design ◽  
Model System ◽  
Nonribosomal Peptide ◽  
Peptide Biosynthesis

scholarly journals Put a Bow on It: Knotted Antibiotics Take Center Stage

Antibiotics ◽  
2019 ◽  
Vol 8 (3) ◽  
pp. 117 ◽  
Author(s):  
Stephanie Tan ◽  
Gaelen Moore ◽  
Justin Nodwell
Keyword(s):  
Current Knowledge ◽  
Chemical Diversity ◽  
Peptide Antibiotics ◽  
Linear Peptide ◽  
Peptidoglycan Biosynthesis ◽  
Lasso Peptides ◽  
Lipid Ii ◽  
Modified Peptides ◽  
Domains Of Life ◽  
Peptide Biosynthesis

Ribosomally-synthesized and post-translationally modified peptides (RiPPs) are a large class of natural products produced across all domains of life. The lasso peptides, a subclass of RiPPs with a lasso-like structure, are structurally and functionally unique compared to other known peptide antibiotics in that the linear peptide is literally “tied in a knot” during its post-translational maturation. This underexplored class of peptides brings chemical diversity and unique modes of action to the antibiotic space. To date, eight different lasso peptides have been shown to target three known molecular machines: RNA polymerase, the lipid II precursor in peptidoglycan biosynthesis, and the ClpC1 subunit of the Clp protease involved in protein homeostasis. Here, we discuss the current knowledge on lasso peptide biosynthesis as well as their antibiotic activity, molecular targets, and mechanisms of action.

Interrupted adenylation domains: unique bifunctional enzymes involved in nonribosomal peptide biosynthesis

2015 ◽  
Vol 32 (5) ◽  
pp. 641-653 ◽  
Author(s):  
Kristin J. Labby ◽  
Stoyan G. Watsula ◽  
Sylvie Garneau-Tsodikova
Keyword(s):  
Amino Acid ◽  
Adenylation Domain ◽  
Nonribosomal Peptide ◽  
Bifunctional Enzymes ◽  
Peptide Biosynthesis ◽  
Single Enzyme

This highlight focuses on one of Nature's key strategies to doubly modify an amino acid during nonribosomal peptide biosynthesis by using a single enzyme, an interrupted adenylation domain.

scholarly journals In Vitro Reconstruction of Nonribosomal Peptide Biosynthesis Directly from DNA Using Cell-Free Protein Synthesis

2016 ◽  
Vol 6 (1) ◽  
pp. 39-44 ◽  
Author(s):  
Anthony W. Goering ◽  
Jian Li ◽  
Ryan A. McClure ◽  
Regan J. Thomson ◽  
Michael C. Jewett ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Nonribosomal Peptide ◽  
Free Protein ◽  
Peptide Biosynthesis ◽  
Cell Free Protein Synthesis
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