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
  • 1. Institute of Medical Sciences, University of Aberdeen, Ashgrove Road West, Foresterhill Aberdeen AB25 2ZD, UK. [email protected].
  • 2. Department of Microbiology, University of Helsinki, P.O.Box 56, Viikki Biocenter, Viikinkaari 9, 00014, Finland. [email protected].
  • 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.

Products