Engineering of lysine cyclodeaminase conformational dynamics for relieving substrate and product inhibitions in the biosynthesis of l-pipecolic acid
Author:
Affiliation:
1. College of Biotechnology and Pharmaceutical Engineering
2. Nanjing Tech University
3. Nanjing
4. China
5. School of Life Sciences and Biotechnology
6. Shanghai Jiaotong University
7. Shanghai
Abstract
Efficient biocatalytic process construction by relieving substrate and product inhibitions via identification and engineering of enzyme conformational dynamics.
Funder
National Natural Science Foundation of China
Publisher
Royal Society of Chemistry (RSC)
Subject
Catalysis
Link
http://pubs.rsc.org/en/content/articlepdf/2019/CY/C8CY02301H
Reference62 articles.
1. Tailoring new enzyme functions by rational redesign
2. De novo design of biocatalysts
3. Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design
4. Engineering of the Conformational Dynamics of an Enzyme for Relieving the Product Inhibition
5. Effect of Overall Feedback Inhibition in Unbranched Biosynthetic Pathways
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1. Biocatalytic Synthesis of l‐Pipecolic Acid by a Lysine Cyclodeaminase: Batch and Flow Reactors;ChemCatChem;2024-04-22
2. Multidimensional engineering of Escherichia coli for efficient biosynthesis of cis-3-hydroxypipecolic acid;Bioresource Technology;2023-08
3. Catalytic Production of Functional Monomers from Lysine and Their Application in High-Valued Polymers;Catalysts;2022-12-27
4. Selective Biocatalytic Defunctionalization of Raw Materials;ChemSusChem;2022-04-19
5. An Artificial Pathway for N-Hydroxy-Pipecolic Acid Production From L-Lysine in Escherichia coli;Frontiers in Microbiology;2022-03-08
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