Enzymatic macrocyclization of ribosomally synthesized and posttranslational modified peptides via C-S and C-C bond formation

被引：12
|
作者：
Lu, Jingxia [1 ]
Li, Yuqing [1 ]
Bai, Zengbing [1 ]
Lv, Hongmei [1 ]
Wang, Huan [1 ]
机构：
[1] Nanjing Univ, Sch Chem & Chem Engn, State Key Lab Coordinat Chem, Chem & Biomed Innovat Ctr,Jiangsu Key Lab Adv Org, Nanjing 210093, Peoples R China
来源：
NATURAL PRODUCT REPORTS | 2021年 / 38卷 / 05期
关键词：
SIDE-RING-SYSTEM; RADICAL SAM ENZYMES; SUBSTRATE-SPECIFICITY; APOPTOSIS INDUCER; BACILLUS-SUBTILIS; CRYSTAL-STRUCTURE; DURAMYCIN-B; THURICIN CD; BIOSYNTHESIS; PROTEIN;
D O I：
10.1039/d0np00044b
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Covering: 2000 to 2020 Ribosomally synthesized and posttranslational modified peptides (RiPPs) are a rapidly growing class of bioactive natural products. Many members of RiPPs contain macrocyclic structural units constructed by modification enzymes through macrocyclization of linear precursor peptides. In this study, we summarize recent progress in the macrocyclization of RiPPs by C-S and C-C bond formation with a focus on the current understanding of the enzymatic mechanisms.
引用
收藏
页码：981 / 992
页数：12
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