文献类型：期刊文献

英文题名：Structure-guided engineering of Pseudomonas dacunhael-aspartate β-decarboxylase for l-homophenylalanine synthesis

作者：Zhang, Min[1];Hu, Pengfei[2];Zheng, Yu-Cong[1];Zeng, Bu-Bing[2];Chen, Qi[1];Zhang, Zhi-Jun[1];Xu, Jian-He[1]

机构：[1]East China Univ Sci & Technol, Shanghai Collaborat Innovat Ctr Biamfg, State Key Lab Bioreactor Engn, Sch Biotechnol, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, Shanghai Key Lab New Drug Design, Shanghai 200237, Peoples R China

年份：2020

卷号：56

期号：89

起止页码：13876

外文期刊名：CHEMICAL COMMUNICATIONS

收录：;EI(收录号：20204709500965);WOS:【SCI-EXPANDED(收录号:WOS:000588197200034)】；

基金：This work was financially supported by the National Natural Science Foundation of China (No. 21536004, 21871085 & 32071475), the Natural Science Foundation of Shanghai (No. 18ZR1408400), the National Key Research and Development Program of China (No. 2019YFA0905000 & 2018YFC1706200), and the Fundamental Research Funds for the Central Universities (No. 22221818014).

语种：英文

外文关键词：Positive ions

摘要：Structure-guided engineering of Pseudomonas dacunhael-aspartate beta-decarboxylase (AspBDC) resulted in a double mutant (R37A/T382G) with remarkable 15 400-fold improvement in specific activity reaching 216 mU mg(-1), towards the target substrate 3(R)-benzyl-l-aspartate. A novel strategy for enzymatic synthesis of l-homophenylalanine was developed by using the variant as a biocatalyst affording 75% product yield within 12 h. Our results underscore the potential of engineered AspBDC for the biocatalytic synthesis of pharmaceutically relevant and value added unnatural l-amino acids.