Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway.
Chem Commun (Camb), 2022/10/27;58(86):12054-12057.
Clemente C[1], Johnson N[1], Ouyang X[2], Popin RV[2], Dall'Angelo S[1], Wahlsten M[2], Jokela J[2], Colombano A[1], Nardone B[3], Fewer DP[2], Houssen WE[1, 4]
Affiliations
PMID: 36193595DOI: 10.1039/d2cc01799g
Impact factor: 6.065
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.
MeSH terms
Biosynthetic Pathways; Dimethylallyltranstransferase; Arginine; Homoarginine; Guanidine; Peptides, Cyclic
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