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Updated: Apr 30, 2026

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
Enzymatic synthesis of L-norephedrine by coupling recombinant pyruvate decarboxylase and ω-transaminase
Xuri Wu1, Mengdan Fei, Yong Chen
1State Key Laboratory of Natural Medicines and Laboratory of Chemical Biology, China Pharmaceutical University, 24 Tongjia St., Nanjing, Jiangsu Province, 210009, People's Republic of China.
Abstract:
L-Norephedrine, a natural plant alkaloid, possesses similar activity as ephedrine and can be used as a vicinal amino alcohol for the asymmetric synthesis of a variety of optically pure compounds, including pharmaceuticals, fine chemicals, and agrochemicals. Because of the existence of two asymmetric centers, efficient synthesis of L-norephedrine has been challenging. In the present study, an R-selective pyruvate decarboxylase from Saccharomyces cerevisiae and an S-selective ω-transaminase from Vibrio fluvialis JS17 were coupled to develop a sequential process for the stereoselective biosynthesis of L-norephedrine. After systematic optimization of the reaction conditions, a green, economic, and practical biocatalytic method to prepare L-norephedrine was established to achieve de and ee values of greater than 99.5 % and a molar yield over 60 %. The present coupling approach can facilitate the development of sequential reactions by various biocatalysts.
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