Molecular Evolution of an Aminotransferase Based on Substrate–Enzyme Binding Energy Analysis for Efficient Valienamine Synthesis-Reference-Cited by-同舟云学术

Molecular Evolution of an Aminotransferase Based on Substrate–Enzyme Binding Energy Analysis for Efficient Valienamine Synthesis

Published:2022-10-25 Issue:21 Volume:12 Page:13703-13714
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Cui Li¹^ORCID,Cui Anqi¹,Li Qitong¹,Yang Lezhou¹,Liu Hao¹,Shao Wenguang¹,Feng Yan¹^ORCID

Affiliation:

1. State Key Laboratory of Microbial Metabolism, School of Life Science & Biotechnology, and Joint International Research Laboratory of Metabolic & Developmental Sciences, Shanghai Jiao Tong University, Shanghai 200240, China

Funder

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

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.2c03784

Reference58 articles.

1. Development and Medical Application of Unsaturated Carbaglycosylamine Glycosidase Inhibitors

2. Biotechnology and molecular biology of the ?-glucosidase inhibitor acarbose

3. Trehalase inhibition by validamycin A may be a promising target to design new fungicides and insecticides

4. Biosynthesis of Unusual Aminocyclitol-Containing Natural Products

5. Biosynthesis of nitrogen-containing natural products, C7N aminocyclitols and bis-indoles, from actinomycetes

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