Projects per year
Abstract
Cyanobactins are a diverse collection of natural products that originate from short peptides made on a ribosome. The amino acids are modified in a series of transformations catalyzed by multiple enzymes. The patellamide pathway is the most well studied and characterized example. Here we review the structures and mechanisms of the enzymes that cleave peptide bonds, macrocyclise peptides, heterocyclise cysteine (as well as threonine and serine) residues, oxidize five-membered heterocycles and attach prenyl groups. Some enzymes operate by novel mechanisms which is of interest and in addition the enzymes uncouple recognition from catalysis. The normally tight relationship between these factors hinders biotechnology. The cyanobactin pathway may be particularly suitable for exploitation, with progress observed with in vivo and in vitro approaches.
Original language | English |
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Pages (from-to) | 80-88 |
Number of pages | 9 |
Journal | Current Opinion in Chemical Biology |
Volume | 35 |
Early online date | 14 Sept 2016 |
DOIs | |
Publication status | Published - Dec 2016 |
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Dive into the research topics of 'Mechanisms of cyanobactin biosynthesis'. Together they form a unique fingerprint.Projects
- 2 Finished
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Exploring the mechanism: Exploring the mechanism and scope of the enzymatic formation of five membered ring
Naismith, J. (PI), Botting, C. H. (CoI), Koehnke, J. A. J. G. (CoI) & Schwarz-Linek, U. (CoI)
1/10/13 → 30/09/17
Project: Standard