Exploring the Catalytic Promiscuity of a New Glycosyltransferase from Carthamus tinctorius-Reference-Cited by-同舟云学术

Exploring the Catalytic Promiscuity of a New Glycosyltransferase from Carthamus tinctorius

Published:2014-09-05 Issue:18 Volume:16 Page:4874-4877
ISSN:1523-7060
Container-title:Organic Letters
language:en
Short-container-title:Org. Lett.

Author:

Xie Kebo¹,Chen Ridao¹,Li Jianhua¹,Wang Ruishan¹,Chen Dawei¹,Dou Xiaoxiang¹,Dai Jungui¹

Affiliation:

1. State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, 1 Xian Nong Tan Street, Beijing 100050, P.R. China

Funder

Ministry of Education of the People's Republic of China

Ministry of Science and Technology of the People's Republic of China

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ol502380p

Reference45 articles.

1. The role of carbohydrates in biologically active natural products

2. Natures Carbohydrate Chemists The Enzymatic Glycosylation of Bioactive Bacterial Metabolites

3. Saponins in cereals

4. Colchicine Glycorandomization Influences Cytotoxicity and Mechanism of Action

5. The C-Glycosyltransferase UrdGT2 Is Unselective toward d- and l-Configured Nucleotide-Bound Rhodinoses

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