Yunfeng Cui
Chinese Academy of Sciences
29 Papers
36 Citations
Yunfeng Cui is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Chemistry & Catalysis. The author has an hindex of 7, co-authored 19 publications.
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Papers
Structure, function and inhibition of ent -kaurene synthase from Bradyrhizobium japonicum
Wenting Liu,Xinxin Feng,Yingying Zheng,Chun-Hsiang Huang,Chiaki Nakano,Tsutomu Hoshino,Shannon Bogue,Tzu-Ping Ko,Chun-Chi Chen,Yunfeng Cui,Jian Li,Iren Wang,Shang-Te Danny Hsu,Eric Oldfield,Rey-Ting Guo +14 more
TL;DR: The first X-ray crystal structure of ent-kaur-16-ene synthase from Bradyrhizobium japonicum is reported, providing insights into catalytic activity, as well as structural comparisons with diverse terpene synthases and cyclases which clearly separate the terPene cyclases from other terpenes synthases having highly α-helical structures.
A new D-threonine aldolase as a promising biocatalyst for highly stereoselective preparation of chiral aromatic β-hydroxy-α-amino acids
TL;DR: It was found that the conversion and Cβ-stereoselectivity were dramatically influenced by the reaction temperature, co-solvent, amount of enzyme and reaction time, and it was possible to enable the reaction under kinetic control to retain suitable conversion and high stereoselectivities at the β-carbon, thus tackling the “Cβ-Stereoselectedivity problem”.
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Inverting the Enantiopreference of Nitrilase-Catalyzed Desymmetric Hydrolysis of Prochiral Dinitriles by Reshaping the Binding Pocket with a Mirror-Image Strategy
Shanshan Yu,Jinlong Li,Peiyuan Yao,Jinhui Feng,Yunfeng Cui,Jianjiong Li,Liu Xiangtao,Qiaqing Wu,Jianping Lin,Dunming Zhu +9 more
TL;DR: This study may offer a general strategy to switch the stereopreference of other nitrilases and other classes of enzymes toward the desymmetric reactions of prochiral substrates with two identical reactive functional groups, that are often desirable in asymmetric synthesis.
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Structure-Guided Directed Evolution of a Carbonyl Reductase Enables the Stereoselective Synthesis of (2S,3S)-2,2-Disubstituted-3-hydroxycyclopentanones via Desymmetric Reduction.
Juan Li,Jinhui Feng,Xi Chen,Jingyao Gong,Yunfeng Cui,Hongliu Zhang,Bu Dandan,Qiaqing Wu,Dunming Zhu +8 more
TL;DR: In this article, an engineered carbonyl reductase (M4) was obtained through structure-guided directed evolution of a SSCR from Sporobolomyces salmonicolor AKU4429, which showed 23.9fold enhancement of enzyme activity toward the model substrate 2-methyl-2-benzyl-1,3-cyclopentanedione, affording the (2S, 3S)-stereoisomer in >98% ratio.
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Efficient Biosynthesis of (R)‐ or (S)‐2‐Hydroxybutyrate from l‐Threonine through a Synthetic Biology Approach
TL;DR: This one-pot multi-enzyme transformation provides a new practical method for the synthesis of these important optically pure compounds and was developed by using recombinant Escherichia coli cells expressing separately or co-expressing l-threonine deaminase.
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