Biosynthesis of thiopeptide antibiotics and their pathway engineering
- 19 December 2012
- journal article
- review article
- Published by Royal Society of Chemistry (RSC) in Natural Product Reports
- Vol. 30 (2), 218-226
- https://doi.org/10.1039/c2np20107k
Abstract
Covering: 2009 to 2012 Thiopeptide antibiotics, a growing class of highly modified polythiazolyl peptides, have long been known for their remarkable bioactivities and unusual modes of actions. Uncovering of the ribosomal origin of thiopeptides now sets the stage for appreciating the initially undervalued modifications of the precursor peptides to afford the astonishing structure complexity. In this Highlight, we discuss the advances during the past four years in understanding the generality and specificity of thiopeptide biosynthesis, and on this basis, in expanding the structural diversity by pathway engineering.Keywords
This publication has 63 references indexed in Scilit:
- Recent Advances in the Chemistry and Biology of Naturally Occurring AntibioticsAngewandte Chemie-International Edition, 2009
- Translational Regulation via L11: Molecular Switches on the Ribosome Turned On and Off by Thiostrepton and MicrococcinMolecular Cell, 2008
- From Amino Acids to Heteroaromatics—Thiopeptide Antibiotics, Nature's Heterocyclic PeptidesAngewandte Chemie-International Edition, 2007
- Elongation factor Tu‐targeted antibiotics: Four different structures, two mechanisms of actionFEBS Letters, 2006
- Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu,Biochemistry, 2006
- Thiopeptide AntibioticsChemical Reviews, 2005
- Structural Basis for Contrasting Activities of Ribosome Binding Thiazole AntibioticsCell Chemical Biology, 2003
- Structure of an EF-Tu Complex with a Thiazolyl Peptide Antibiotic Determined at 2.35 Å Resolution: Atomic Basis for GE2270A Inhibition of EF-Tu,Biochemistry, 1999
- The antibiotic micrococcin acts on protein L11 at the ribosomal GTPase centreJournal of Molecular Biology, 1999
- The antibiotic thiostrepton inhibits a functional transition within protein L11 at the ribosomal GTPase centreJournal of Molecular Biology, 1998