Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Global Station for Biosurfaces and Drug Discovery, Hokkaido University, Kita 12, Nishi 6, Sapporo 060-0812, Japan.
J Am Chem Soc. 2021 Jul 14;143(27):10083-10087. doi: 10.1021/jacs.1c05732. Epub 2021 Jun 28.
Guanidine prenylation is an outstanding modification in alkaloid and peptide biosynthesis, but its enzymatic basis has remained elusive. We report the isolation of argicyclamides, a new class of cyanobactins with unique mono- and bis-prenylations on guanidine moieties, from NIES-88. The genetic basis of argicyclamide biosynthesis was established by the heterologous expression and characterization of biosynthetic enzymes including AgcF, a new guanidine prenyltransferase. This study provides important insight into the biosynthesis of prenylated guanidines and offers a new toolkit for peptide modification.
胍基的prenylation 是生物碱和肽生物合成中的一种突出的修饰，但它的酶学基础仍然难以捉摸。我们从 NIES-88 中分离到了 argicyclamides，这是一类新的 cyanobactins，其胍基上具有独特的单和双 prenylations。通过异源表达和 biosynthetic 酶的特性分析，包括一个新的胍基 prenyltransferase AgcF，确定了 argicyclamide 生物合成的遗传基础。这项研究为 prenylated guanidines 的生物合成提供了重要的见解，并为肽修饰提供了一个新的工具包。
