Thiopeptide Antibiotic Biosynthesis

Tailors at work: The structurally intriguing thiopeptide antibiotic natural products have been conclusively and universally shown to be biosynthesized from genetically encoded linear precursor peptides by novel tailoring enzymes. These unique findings challenge previously accepted biosynthesis parad...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2009-09, Vol.48 (37), p.6770-6773
Main Authors: Arndt, Hans-Dieter, Schoof, Sebastian, Lu, Jin-Yong
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Anti-Bacterial Agents - biosynthesis
Anti-Bacterial Agents - chemistry
antibiotics
biosynthesis
Genes, Bacterial
Molecular Sequence Data
Multigene Family
natural products
Peptide Biosynthesis
Peptides, Cyclic - biosynthesis
Peptides, Cyclic - chemistry
ribosomal peptides
Sequence Alignment
Sequence Homology, Amino Acid
Sulfhydryl Compounds - chemistry
thiopeptides
Thiostrepton - biosynthesis
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Summary:Tailors at work: The structurally intriguing thiopeptide antibiotic natural products have been conclusively and universally shown to be biosynthesized from genetically encoded linear precursor peptides by novel tailoring enzymes. These unique findings challenge previously accepted biosynthesis paradigms and are expected to inspire future discoveries in the chemistry and biology of peptide natural products.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200901808