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

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

  • Chem Commun (Camb). 2022 Oct 27;58(86):12054-12057. doi: 10.1039/d2cc01799g.
Claudia Clemente 1,  Nicholas Johnson 1,  Xiaodan Ouyang 2,  Rafael V Popin 2,  Sergio Dall'Angelo 1,  Matti Wahlsten 2,  Jouni Jokela 2,  Alessandro Colombano 1,  Brunello Nardone 3,  David P Fewer 2,  Wael E Houssen 1 4
Affiliations

Affiliations

  • 1 Institute of Medical Sciences, University of Aberdeen, Ashgrove Road West, Foresterhill Aberdeen AB25 2ZD, UK. w.houssen@abdn.ac.uk.
  • 2 Department of Microbiology, University of Helsinki, P.O.Box 56, Viikki Biocenter, Viikinkaari 9, 00014, Finland. david.fewer@helsinki.fi.
  • 3 CEM Microwave Ltd, Buckingham Industrial Park, Buckingham MK18 1WA, UK.
  • 4 Department of Chemistry, University of Aberdeen, Meston Walk, Aberdeen AB24 3UE, UK.
PMID: 36193595 DOI: 10.1039/d2cc01799g
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.

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