Enzymatic O-Glycosylation of Etoposide Aglycone by Exploration of the Substrate Promiscuity for Glycosyltransferases-Reference-Cited by-同舟云学术

Enzymatic O-Glycosylation of Etoposide Aglycone by Exploration of the Substrate Promiscuity for Glycosyltransferases

Published:2019-11-27 Issue:12 Volume:8 Page:2718-2725
ISSN:2161-5063
Container-title:ACS Synthetic Biology
language:en
Short-container-title:ACS Synth. Biol.

Author:

Jia Kai-Zhi¹,Zhu Li-Wen¹,Qu Xudong²^ORCID,Li Shengying³^ORCID,Shen Yuemao³,Qi Qingsheng³,Zhang Youming³,Li Yue-Zhong³^ORCID,Tang Ya-Jie¹³^ORCID

Affiliation:

1. Hubei Key Laboratory of Industrial Microbiology, Hubei Provincial Cooperative Innovation Center of Industrial Fermentation, Key Laboratory of Fermentation Engineering (Ministry of Education), Hubei University of Technology, Wuhan 430068, China

2. Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, School of Pharmaceutical Sciences, Wuhan University, Wuhan 430071, China

3. State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China

Funder

National Natural Science Foundation of China

Hubei Province

Publisher

American Chemical Society (ACS)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Biomedical Engineering,General Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acssynbio.9b00318

Reference38 articles.

1. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone