Abstract
Not only have antibacterial natural products been an important source of life-saving medicines in the 20th century, but they also have played a pivotal role in the growth of biological chemistry as a discipline. In particular, polyketide and peptide natural products have been extremely rich sources of antibacterial agents that modulate essential microbiological functions, such as nucleic acid and protein biosynthesis, or the integrity of the cell envelope. Using four examples from these two antibiotic superfamilies, this thematic minireview series illustrates how natural products are continuing to present fundamental and translational challenges at the chemistry-biology interface.
Highlights
Two decades ago, genetic analysis of the biosynthesis of several prototypical polyketides and nonribosomal peptides revealed the existence of thiotemplate assembly mechanisms for the backbones of these antibiotics
Whereas non-template enzymatic assembly lines have been recognized as the predominant mechanism for peptide antibiotic biosynthesis in bacteria, some natural products, such as lantibiotics and thiopeptides, are ribosomally derived
Bowers discuss the remarkable story of biosynthesis of this class of antibacterial agents that has emerged within only the past few years
Summary
Genetic analysis of the biosynthesis of several prototypical polyketides and nonribosomal peptides revealed the existence of thiotemplate assembly mechanisms for the backbones of these antibiotics. * This minireview will be reprinted in the 2010 Minireview Compendium, which will be available in January, 2011. 1 To whom correspondence should be addressed.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
