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A Unique Tryptophan C‐Prenyltransferase from the Kawaguchipeptin Biosynthetic Pathway |
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| Authors: | Anirudra Parajuli Daniel H Kwak Luca Dalponte Dr Niina Leikoski Tomas Galica Ugochukwu Umeobika Dr Laurent Trembleau Andrew Bent Prof Kaarina Sivonen Matti Wahlsten Dr Hao Wang Dr Ermanno Rizzi Prof Gianluca De?Bellis Prof James Naismith Prof Marcel Jaspars Prof Xinyu Liu Dr Wael Houssen Dr David Peter Fewer |
| Affiliation: | 1. Microbiology and Biotechnology Division, Department of Food and Environmental Sciences, P.O.Box 56, Viikki Biocenter, Viikinkaari 9, 00014, University of Helsinki Finland;2. Department of Chemistry, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260 USA;3. Marine Biodiscovery Centre, Department of Chemistry, University of Aberdeen, Meston Walk, Aberdeen, AB24 3UE UK;4. Institute of Medical Sciences, University of Aberdeen, Aberdeen, AB25 2ZD UK;5. Institute of Microbiology AS CR, v.v.i., Center ALGATECH, T?eboň, Czech Republic;6. University of South Bohemia, Faculty of Science, Department of Ecosystem Biology, ?eské Budějovice, Czech Republic;7. Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife, KY16 9ST UK;8. Institute for Biomedical Technologies (ITB), National Research Council (CNR), via F.lli Cervi 93, Segrate (MI), Italy;9. Pharmacognosy Department, Faculty of Pharmacy, Mansoura University, Mansoura, 35516 Egypt |
| Abstract: | Cyanobactins are a rapidly growing family of linear and cyclic peptides produced by cyanobacteria. Kawaguchipeptins A and B, two macrocyclic undecapeptides reported earlier from Microcystis aeruginosa NIES‐88, are shown to be products of the cyanobactin biosynthetic pathway. The 9 kb kawaguchipeptin (kgp) gene cluster was identified in a 5.26 Mb draft genome of Microcystis aeruginosa NIES‐88. We verified that this gene cluster is responsible for the production of the kawaguchipeptins through heterologous expression of the kgp gene cluster in Escherichia coli. The KgpF prenyltransferase was overexpressed and was shown to prenylate C‐3 of Trp residues in both linear and cyclic peptides in vitro. Our findings serve to further enhance the structural diversity of cyanobactins to include tryptophan‐prenylated cyclic peptides. |
| Keywords: | biosynthesis cyanobactins peptides prenylation prenyltransferases |
