A unique Tryptophan C-prenyltransferase from the kawaguchipeptin biosynthetic pathway

Anirudra Parajuli; Daniel H. Kwak; Luca Dalponte; Niina Leikoski; Tomas Galica; Ugochukwu Umeobika; Laurent Trembleau; Andrew Bent; Kaarina Sivonen; Matti Wahlsten; Hao Wang; Ermanno Rizzi; Gianluca De Bellis; Jim Naismith; Marcel Jaspars; Xinyu Liu; Wael Houssen; David Peter Fewer

doi:10.1002/anie.201509920

A unique Tryptophan C-prenyltransferase from the kawaguchipeptin biosynthetic pathway

Anirudra Parajuli, Daniel H. Kwak, Luca Dalponte, Niina Leikoski, Tomas Galica, Ugochukwu Umeobika, Laurent Trembleau, Andrew Bent, Kaarina Sivonen, Matti Wahlsten, Hao Wang, Ermanno Rizzi, Gianluca De Bellis, Jim Naismith, Marcel Jaspars, Xinyu Liu, Wael Houssen, David Peter Fewer

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	3596-3599
Number of pages	4
Journal	Angewandte Chemie International Edition
Volume	55
Issue number	11
Early online date	5 Feb 2016
DOIs	https://doi.org/10.1002/anie.201509920
Publication status	Published - 7 Mar 2016

Keywords

Biosynthesis
Cyanobactins
Peptides
Prenylation
Prenyltransferases

Access to Document

10.1002/anie.201509920

Naismith_2016_ACIE_Unique_AAM
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. This work is made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at https://dx.doi.org/10.1002/anie.201509920
Accepted author manuscript, 993 KB

Cite this

Parajuli, A., Kwak, D. H., Dalponte, L., Leikoski, N., Galica, T., Umeobika, U., Trembleau, L., Bent, A., Sivonen, K., Wahlsten, M., Wang, H., Rizzi, E., De Bellis, G., Naismith, J., Jaspars, M., Liu, X., Houssen, W., & Fewer, D. P. (2016). A unique Tryptophan C-prenyltransferase from the kawaguchipeptin biosynthetic pathway. Angewandte Chemie International Edition, 55(11), 3596-3599. https://doi.org/10.1002/anie.201509920

@article{885e827e43a64297929af79f643f33a7,

title = "A unique Tryptophan C-prenyltransferase from the kawaguchipeptin biosynthetic pathway",

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",

author = "Anirudra Parajuli and Kwak, {Daniel H.} and Luca Dalponte and Niina Leikoski and Tomas Galica and Ugochukwu Umeobika and Laurent Trembleau and Andrew Bent and Kaarina Sivonen and Matti Wahlsten and Hao Wang and Ermanno Rizzi and Gianluca De Bellis and Jim Naismith and Marcel Jaspars and Xinyu Liu and Wael Houssen and Fewer, {David Peter}",

note = "This work was supported by funding of the Academy of Finland (259505), Helsinki University Research grant (490085) and ESCMID grant (4720572) to D.P.F., University of Pittsburgh Central Research Development Fund to X.L., Technology Strategy Board grant (131181) to W.H., M.J. and J.H.N. National Programme of Sustainability I of the Ministry of Education of the Czech Republic I grant (LO1416) to T.G.",

year = "2016",

month = mar,

day = "7",

doi = "10.1002/anie.201509920",

language = "English",

volume = "55",

pages = "3596--3599",

journal = "Angewandte Chemie International Edition",

issn = "1521-3773",

publisher = "John Wiley & Sons, Ltd",

number = "11",

}

Parajuli, A, Kwak, DH, Dalponte, L, Leikoski, N, Galica, T, Umeobika, U, Trembleau, L, Bent, A, Sivonen, K, Wahlsten, M, Wang, H, Rizzi, E, De Bellis, G, Naismith, J, Jaspars, M, Liu, X, Houssen, W & Fewer, DP 2016, 'A unique Tryptophan C-prenyltransferase from the kawaguchipeptin biosynthetic pathway', Angewandte Chemie International Edition, vol. 55, no. 11, pp. 3596-3599. https://doi.org/10.1002/anie.201509920

TY - JOUR

T1 - A unique Tryptophan C-prenyltransferase from the kawaguchipeptin biosynthetic pathway

AU - Parajuli, Anirudra

AU - Kwak, Daniel H.

AU - Dalponte, Luca

AU - Leikoski, Niina

AU - Galica, Tomas

AU - Umeobika, Ugochukwu

AU - Trembleau, Laurent

AU - Bent, Andrew

AU - Sivonen, Kaarina

AU - Wahlsten, Matti

AU - Wang, Hao

AU - Rizzi, Ermanno

AU - De Bellis, Gianluca

AU - Naismith, Jim

AU - Jaspars, Marcel

AU - Liu, Xinyu

AU - Houssen, Wael

AU - Fewer, David Peter

N1 - This work was supported by funding of the Academy of Finland (259505), Helsinki University Research grant (490085) and ESCMID grant (4720572) to D.P.F., University of Pittsburgh Central Research Development Fund to X.L., Technology Strategy Board grant (131181) to W.H., M.J. and J.H.N. National Programme of Sustainability I of the Ministry of Education of the Czech Republic I grant (LO1416) to T.G.

PY - 2016/3/7

Y1 - 2016/3/7

N2 - 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.

AB - 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.

KW - Biosynthesis

KW - Cyanobactins

KW - Peptides

KW - Prenylation

KW - Prenyltransferases

UR - http://onlinelibrary.wiley.com/wol1/doi/10.1002/anie.201509920/suppinfo

U2 - 10.1002/anie.201509920

DO - 10.1002/anie.201509920

M3 - Article

SN - 1521-3773

VL - 55

SP - 3596

EP - 3599

JO - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

IS - 11

ER -

A unique Tryptophan C-prenyltransferase from the kawaguchipeptin biosynthetic pathway

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Exploring the mechanism: Exploring the mechanism and scope of the enzymatic formation of five membered ring

Cite this

A unique Tryptophan C-prenyltransferase from the kawaguchipeptin biosynthetic pathway

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Projects

Exploring the mechanism: Exploring the mechanism and scope of the enzymatic formation of five membered ring

Cite this