Preparation of Optically Active Alkoxy-serines from Amino-amide Racemate Catalyzed by Escherichia coli Cells with Peptidase B Activity
Preparation of Optically Active Alkoxy-serines from Amino-amide Racemate Catalyzed by Escherichia coli Cells with Peptidase B Activity作者机构：State Key Laboratory of Pharmaceutical Biotechnology School of Life Science Nanjing University Nanjing 210093 P. R. China
出 版 物：《Chemical Research in Chinese Universities》 (高等学校化学研究（英文版）)
年 卷 期：2013年第29卷第1期
页 面：95-98页
核心收录：
学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081703[工学-生物化工] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 0836[工学-生物工程] 082203[工学-发酵工程] 0822[工学-轻工技术与工程]
基 金：Supported by the National Technology-Innovation Fund of China the Open Fund of State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, China
主 题：Alkoxy-serine DL-β-Alkoxy-a-amino propionamide Enzymatic resolution Peptidase B
摘 要：Alkoxy-L-serines are useful for peptide syntheses. The demand for alkoxy-L-serines in the pharmaceutical industries continues to increase because of their multiple physiological effects. In this research, an improved method for alkoxy-L-serines synthesis is reported. A series of substrates, DL-fl-alkoxy-a-amino propionamides, was used for the synthesis of alkoxy-serines catalyzed by Escherichia coli cells with peptidase B（PepB） activity. The results show that PepB has a high resolution activity with DL-fl-alkoxy-a-amino propionamides as substrate. Reaction conditions were optimized, i.e., DL-β-methoxy-a-amino propionamide as substrate at pH=9.0, 40 ℃ and 14 h, and the optimal reaction concentration is 400 mmol/L. The results also show that divalent metal cations exhibit different effects on the PepB activity, for example, Zn2＋ and Cu2＋ can obviously inhibit the activity of PepB, whereas Co2＋, Ca2＋, Mn〉 and Mg2＋ at low concentrations can activate PepB. This research provides access to enantiomerically enriched and valuable alkoxy-L-serines from a simple amino-amide racemate.
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