4.7 Article

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

Journal

CHEMICAL COMMUNICATIONS
Volume 58, Issue 86, Pages 12054-12057

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/d2cc01799g

Keywords

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Funding

  1. EPSRC [EP/S027246/1]
  2. BBSRC [BB/V509206/1]
  3. Novo Nordisk Foundation [18OC0034838]
  4. NordForsk NCoE program NordAqua'' [82845]
  5. University of Aberdeen
  6. China Scholarship Council [201906150148]
  7. IBioIC CTP PhD programme
  8. Doctoral Programme in Microbiology and Biotechnology of the University of Helsinki

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The prenyl-D-Arg-containing autum-nalamide A is identified as a member of the cyanobactin family, and the AutF prenyltransferase can target the guanidinium moiety in arginine and homoarginine, making it a useful tool for biotechnological applications.
Cyanobactins are linear and cyclic post-translationally modified peptides. Here we show that the prenyl-D-Arg-containing autum-nalamide 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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