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

Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway.
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DOI:
10.1039/d2cc01799g
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发表时间:
2022-10-27
影响因子:
4.9
通讯作者:
Houssen, Wael E.
Houssen, Wael E.
中科院分区:
化学2区
文献类型:
--
作者:
Clemente, Claudia;Johnson, Nicholas;Ouyang, Xiaodan;Popin, Rafael, V;Dall'Angelo, Sergio;Wahlsten, Matti;Jokela, Jouni;Colombano, Alessandro;Nardone, Brunello;Fewer, David P.;Houssen, Wael E.

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蓝菌素是线性和环状翻译后修饰的肽。在这里,我们证明含有异戊二烯基-d-Arg 的Autumnalamide A 是氰菌素家族的一员。生化测定表明,AutF 异戊二烯基转移酶以精氨酸和高精氨酸中的胍基部分为目标,是生物技术应用的有用工具。秋酰胺途径中异戊二烯基转移酶 (AutF) 的生化特征表明,它的目标是精氨酸和高精氨酸中胍基部分的氮。
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. Biochemical characterization of the prenyltransferase (AutF) from the autumnalamide pathway shows it targets the nitrogen of the guanidinium moiety in arginine and homoarginine.
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