Reshaping the Substrate Binding Pocket of β-Amino Acid Dehydrogenase for the Synthesis of Aromatic β-Amino Acids

被引:0
|
作者
Liu, Na [1 ]
Feng, Jinhui [1 ]
Chen, Xi [1 ]
Luo, Yuyang [1 ,2 ]
Lv, Tong [1 ]
Wu, Qiaqing [1 ]
Zhu, Dunming [1 ]
机构
[1] Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Natl Engn Res Ctr Ind Enzymes, Tianjin Engn Res Ctr Biocatalyt Technol,Key Lab En, Tianjin 300308, Peoples R China
[2] Tianjin Univ Sci & Technol, Sch Biotechnol, State Key Lab Food Nutr & Safety, Key Lab Ind Fermentat Microbiol,Minist Educ, Tianjin 300457, Peoples R China
基金
国家重点研发计划; 中国国家自然科学基金;
关键词
CATALYTIC ASYMMETRIC-SYNTHESIS; PEPTIDE;
D O I
10.1021/acs.orglett.3c03366
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
By reshaping the substrate-binding pocket of beta-amino acid dehydrogenase (beta-AADH), some variants were obtained with up to 2560-fold enhanced activity toward the model substrates (S)-beta-homophenylalanine and (R)-beta-phenylalanine. A few aromatic beta-amino acids were prepared with >99% ee and high isolated yields via either kinetic resolution of racemates or reductive amination of the corresponding beta-keto acids. This work expands the catalytic capability of beta-AADHs and highlights their practical application in the synthesis of pharmaceutically relevant beta-amino acids.
引用
收藏
页码:8469 / 8473
页数:5
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