Mechanistic investigation of B12-independent glycerol dehydratase and its activating enzyme GD-AE-Reference-Cited by-同舟云学术

Mechanistic investigation of B12-independent glycerol dehydratase and its activating enzyme GD-AE

Published:2022 Issue:16 Volume:58 Page:2738-2741
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Li Yaoyang¹^ORCID,Yao Yadi¹,Yu Lu²^ORCID,Tian Changlin²³^ORCID,Dong Min¹^ORCID

Affiliation:

1. Frontiers Science Center for Synthetic Biology, Key Laboratory of Systems Bioengineering (MOE), School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China

2. High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui 230031, China

3. The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, and Center for Bioanalytical Chemistry, Hefei National Laboratory of Physical Science at Microscale, University of Science and Technology of China, Hefei, Anhui 230026, China

Abstract

GD-AE is a classical radical SAM enzyme that cleaves SAM to form 5′-deoxyadenosine (5′-dA) and a glycyl radical on B12-independent GD. GD catalyzes the glycerol dehydration reaction by direct elimination of the 2-OH group rather than migration.

Funder

National Natural Science Foundation of China

Natural Science Foundation of Tianjin City

Chinese Academy of Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CC/D1CC06991H

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2. Correction: Mechanistic investigation of B12-independent glycerol dehydratase and its activating enzyme GD-AE;Chemical Communications;2022