Reaction mechanism and regioselectivity of uridine diphosphate glucosyltransferase RrUGT3: a combined experimental and computational study-Reference-Cited by-同舟云学术

Reaction mechanism and regioselectivity of uridine diphosphate glucosyltransferase RrUGT3: a combined experimental and computational study

Published:2024 Issue:17 Volume:14 Page:4882-4895
ISSN:2044-4753
Container-title:Catalysis Science & Technology
language:en
Short-container-title:Catal. Sci. Technol.

Author:

Li Mengsha¹²^ORCID,You Cai³⁴⁵,Guo Fei³,Han Qingfang¹²,Xie Xixian¹,Ma Lijuan¹,Li Shengying³^ORCID,Du Lei³^ORCID,Sheng Xiang²⁶^ORCID,Su Hao²⁶^ORCID

Affiliation:

1. College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, P. R. China

2. Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, P. R. China

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

4. Shandong Provincial Key Laboratory of Synthetic Biology, CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, Shandong, P. R. China

5. Shandong Energy Institute, Qingdao 266101, P. R. China

6. National Center of Technology Innovation for Synthetic Biology, National Engineering Research Center of Industrial Enzymes and, Key Laboratory of Engineering Biology for Low-Carbon Manufacturing, Tianjin 300308, P. R. China

Abstract

A substrate binding induced conformational change was found to be essential for the occurrence of RrUGT3 catalyzed transglycosylation reactions.

Funder

National Natural Science Foundation of China

National Key Research and Development Program of China

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/CY/D4CY00721B

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