Discovery of a New Family of Dieckmann Cyclases Essential to Tetramic Acid and Pyridone-Based Natural Products Biosynthesis

被引：42
|
作者：
Gui, Chun [1 ,2 ]
Li, Qinglian [1 ]
Mo, Xuhua [1 ,3 ]
Qin, Xiangjing [1 ]
Ma, Junying [1 ]
Ju, Jianhua [1 ]
机构：
[1] Chinese Acad Sci, CAS Key Lab Trop Marine Bioresources & Ecol, Guangdong Key Lab Marine Mat Med, RNAM Ctr Marine Microbiol,South China Sea Inst Oc, Guangzhou 510301, Guangdong, Peoples R China
[2] Univ Chinese Acad Sci, Beijing 110039, Peoples R China
[3] Qingdao Agr Univ, Sch Life Sci, Shandong Key Lab Appl Mycol, Qingdao 266109, Peoples R China
来源：
ORGANIC LETTERS | 2015年 / 17卷 / 03期
关键词：
GENE-CLUSTER; THIOESTERASE DOMAIN; TIRANDAMYCIN BIOSYNTHESIS; POLYKETIDE SYNTHASE; CRYSTAL-STRUCTURE; STREPTOLYDIGIN; IDENTIFICATION; METABOLITES; DERIVATIVES; ACTIVATION;
D O I：
10.1021/ol5036497
中图分类号：
O62 [有机化学];
学科分类号：
070303 ; 081704 ;
摘要：
Bioinformatic analyses indicate that TrdC, SlgL, LipX(2), KirHI, and FacHI belong to a group of highly homologous proteins involved in biosynthesis of actinomycete-derived tirandamycin B, streptolydigin, alpha-lipomycin, kirromycin, and factumycin, respectively. However, assignment of their biosynthetic roles has remained elusive. Gene inactivation and complementation, in vitro biochemical assays with synthetic analogues, point mutations, and phylogenetic tree analyses reveal that these proteins represent a new family of Dieckmann cyclases that drive tetramic acid and pyridone scaffold biosynthesis.
引用
收藏
页码：628 / 631
页数：4
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