Biochemical Characterization of a Cyanobactin Arginine-N-Prenylase from the Autumnalamide Biosynthetic Pathway

Claudia Clemente, Nicholas Ross Johnson, Xiaodan Ouyang, Rafael V. Popin, Sergio Dall'Angelo, Matti Wahlsten, Jouni Jokela, Alessandro Colombano, Brunello Nardone, David Peter Fewer* (Corresponding Author), Wael E Houssen* (Corresponding Author)

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)
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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 demonstate that the AutF prenyltransferase
targets the guanidinium moiety in arginine and homoarginine and is a useful tool for biotechnological applications.
Original languageEnglish
Pages (from-to)12054-12057
Number of pages4
JournalChemical Communications
Issue number86
Early online date28 Sept 2022
Publication statusPublished - 7 Nov 2022

Bibliographical note

This project was supported by a fellowship grant from the
EPSRC (no. EP/S027246/1, W.E.H.), a training grant from the
BBSRC (BB/V509206/1, W.E.H. and S.D.), the Novo Nordisk
Foundation (18OC0034838, D.P.F.) and the NordForsk NCoE
program “NordAqua” (Project Number 82845, D.P.F.). CC is
funded by a PhD studentship from University of Aberdeen. NJ is
funded by the IBioIC CTP PhD programme. RVP was funded by
the Doctoral Programme in Microbiology and Biotechnology of
the University of Helsinki. XO was funded by the China
Scholarship Council (Grant 201906150148). We are grateful to
Professor James Naismith (University of Oxford) for sharing the
construct used to express the macrocyclase PCY1. We thank Dr
Huanting Liu (University of St Andrews) for sharing the

Data Availability Statement

Electronic supplementary information (ESI) available: Experimental section,
Fig. S1-S37 and Tables S1-S5. See DOI:


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