Preparation of Optically Active Alkoxy-serines from Amino-amide Racemate Catalyzed by Escherichia coli Cells with Peptidase B Activity

• Published in: Chemical research in Chinese universities Vol. 29; no. 1; pp. 95 - 98
• Main Authors: Wang, Zhi-yuan, Liu, Jun-zhong, Xu, Li-sheng, Zhang, Hong-juan, Liu, Qian, Jiao, Qing-cai
• Format: Journal Article
• Language: English
• Published: Heidelberg Jilin University and The Editorial Department of Chemical Research in Chinese Universities 01.02.2013
• Subjects: Analytical Chemistry; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Inorganic Chemistry; L-丝氨酸; Organic Chemistry; Physical Chemistry; α-氨基; 丙酰胺; 光学活性; 外消旋体; 大肠杆菌细胞; 烷氧基; 肽酶; Enzymatic resolution; Peptidase B; Alkoxy-serine; amino propionamide; -; Alkoxy
• ISSN: 1005-9040; 2210-3171
• DOI: 10.1007/s40242-012-2249-2

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.