Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway

Claudia Clemente; Nicholas Johnson; Xiaodan Ouyang; Rafael V. Popin; Sergio Dall'Angelo; Matti Wahlsten; Jouni Jokela; Alessandro Colombano; Brunello Nardone; David P. Fewer; Wael E. Houssen

doi:10.1039/D2CC01799G

Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway†

Claudia Clemente,

^a Nicholas Johnson,

^a Xiaodan Ouyang,

^b Rafael V. Popin,

^b Sergio Dall'Angelo,

^a Matti Wahlsten,

^b Jouni Jokela,^b Alessandro Colombano,

^a Brunello Nardone,^c David P. Fewer

*^b and Wael E. Houssen

*^ad

Author affiliations

* Corresponding authors

^a Institute of Medical Sciences, University of Aberdeen, Ashgrove Road West, Foresterhill Aberdeen AB25 2ZD, UK
E-mail: w.houssen@abdn.ac.uk

^b Department of Microbiology, University of Helsinki, P.O.Box 56, Viikki Biocenter, Viikinkaari 9, Finland
E-mail: david.fewer@helsinki.fi

^c CEM Microwave Ltd, Buckingham Industrial Park, Buckingham MK18 1WA, UK

^d Department of Chemistry, University of Aberdeen, Meston Walk, Aberdeen AB24 3UE, UK

Abstract

Cyanobactins are linear and cyclic post-translationally modified peptides. Here we show that the prenyl-D-Arg-containing autumnalamide A is a member of the cyanobactin family. Biochemical assays demonstrate that the AutF prenyltransferase targets the guanidinium moiety in arginine and homoarginine and is a useful tool for biotechnological applications.

Chemical Communications

Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway†

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Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway

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