scholarly journals Mining methods and typical structural mechanisms of terpene cyclases

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Zheng-Yu Huang ◽  
Ru-Yi Ye ◽  
Hui-Lei Yu ◽  
Ai-Tao Li ◽  
Jian-He Xu

AbstractTerpenoids, formed by cyclization and/or permutation of isoprenes, are the most diverse and abundant class of natural products with a broad range of significant functions. One family of the critical enzymes involved in terpenoid biosynthesis is terpene cyclases (TCs), also known as terpene synthases (TSs), which are responsible for forming the ring structure as a backbone of functionally diverse terpenoids. With the recent advances in biotechnology, the researches on terpene cyclases have gradually shifted from the genomic mining of novel enzyme resources to the analysis of their structures and mechanisms. In this review, we summarize both the new methods for genomic mining and the structural mechanisms of some typical terpene cyclases, which are helpful for the discovery, engineering and application of more and new TCs.

2019 ◽  
Vol 16 (5) ◽  
pp. 422-452 ◽  
Author(s):  
Dau Xuan Duc

Furans are five-membered aromatic heterocycles containing one oxygen atom that are important building blocks in organic chemistry, but also as natural products found in various natural sources, mostly in plants, algae and microorganisms. In this review, we discussed recent advances in the synthesis of furan compounds. Some classical methods have been modified and improved, while other new methods have been developed. A vast variety of catalysts was used for these transformations. In many studies, furan synthesis reaction mechanisms were also investigated and proposed.


ChemInform ◽  
2010 ◽  
Vol 30 (21) ◽  
pp. no-no
Author(s):  
K. C. Nicolaou ◽  
M. H. D. Postema ◽  
N. D. Miller

2010 ◽  
Vol 27 (12) ◽  
pp. 1781 ◽  
Author(s):  
Inder Pal Singh ◽  
Hardik S. Bodiwala

2021 ◽  
Author(s):  
Ankur Sarkar ◽  
Edward Kim ◽  
Taehwan Jang ◽  
Akarawin Hongdusit ◽  
Hyungjun Kim ◽  
...  

Abstract The design of small molecules that inhibit disease-relevant proteins represents a longstanding challenge of medicinal chemistry. Here, we describe an approach for encoding this challenge—the inhibition of a human drug target—into a microbial host and using it to guide the discovery and biosynthesis of targeted, biologically active natural products. This approach identified two previously unknown terpenoid inhibitors of protein tyrosine phosphatase 1B (PTP1B), an elusive therapeutic target for the treatment of diabetes and cancer. Both inhibitors appear to target an allosteric site, which confers selectivity, and can inhibit PTP1B in living cells. A screen of 24 uncharacterized terpene synthases from a pool of 4,464 genes uncovered additional hits, demonstrating a scalable discovery approach, and the incorporation of different PTPs into the microbial host yielded alternative PTP-specific detection systems. Findings illustrate the potential for using microbes to discover and build natural products that exhibit precisely defined biochemical activities yet possess unanticipated structures and/or binding sites.


2018 ◽  
Vol 5 (6) ◽  
pp. 1049-1066 ◽  
Author(s):  
Yingbo Shi ◽  
Qiaoling Wang ◽  
Shuanhu Gao

This review focuses on selected applications of the intramolecular Mannich reaction as a key step in the total synthesis of natural products (2000–2017).


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