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A Unique Tryptophan C‐Prenyltransferase from the Kawaguchipeptin Biosynthetic Pathway
Author(s) -
Parajuli Anirudra,
Kwak Daniel H.,
Dalponte Luca,
Leikoski Niina,
Galica Tomas,
Umeobika Ugochukwu,
Trembleau Laurent,
Bent Andrew,
Sivonen Kaarina,
Wahlsten Matti,
Wang Hao,
Rizzi Ermanno,
De Bellis Gianluca,
Naismith James,
Jaspars Marcel,
Liu Xinyu,
Houssen Wael,
Fewer David Peter
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201509920
Subject(s) - prenyltransferase , gene cluster , chemistry , heterologous expression , tryptophan , cyclic peptide , escherichia coli , prenylation , gene , biochemistry , microcystis aeruginosa , biosynthesis , heterologous , cyanobacteria , biology , peptide , genetics , enzyme , amino acid , recombinant dna , bacteria
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.