Circular Logic: Nonribosomal Peptide-like Macrocyclization with a Ribosomal Peptide Catalyst
- 20 October 2010
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 132 (44), 15499-15501
- https://doi.org/10.1021/ja1067806
Abstract
A protease from ribosomal peptide biosynthesis macrocyclizes diverse substrates, including those resembling nonribosomal peptide and hybrid polyketide−peptide products. The proposed mechanism is analogous to thioesterase-catalyzed chemistry, but the substrates are amide bonds rather than thioesters.This publication has 15 references indexed in Scilit:
- Cyclotides as templates in drug designDrug Discovery Today, 2010
- Cyanobactins – Ubiquitous Cyanobacterial Ribosomal Peptide MetabolitesPublished by Elsevier BV ,2010
- Insights into the Biosynthesis and Stability of the Lasso Peptide CapistruinCell Chemical Biology, 2009
- Using Marine Natural Products to Discover a Protease that Catalyzes Peptide Macrocyclization of Diverse SubstratesJournal of the American Chemical Society, 2009
- Ribosomal Synthesis of Tricyclic Depsipeptides in Bloom‐Forming CyanobacteriaAngewandte Chemie, 2008
- A global assembly line for cyanobactinsNature Chemical Biology, 2008
- Two Enzymes Catalyze the Maturation of a Lasso Peptide in Escherichia coliCell Chemical Biology, 2007
- Macrocyclization strategies in polyketide and nonribosomal peptide biosynthesisNatural Product Reports, 2007
- Natural combinatorial peptide libraries in cyanobacterial symbionts of marine ascidiansNature Chemical Biology, 2006
- How Structural Features Influence the Biomembrane Permeability of PeptidesJournal of Pharmaceutical Sciences, 1996