7607-72-9Relevant articles and documents
A novel strategy for efficient chemoenzymatic synthesis of D-glutamine using recombinant Escherichia coli cells
Du, Qinglin,Zhang, Xiangyang,Pan, Xinru,Zhang, Hongjuan,Yang, Yu-Shun,Liu, Junzhong,Jiao, Qingcai
, (2020/06/17)
D-glutamine is a D type stereoisomer of glutamine which is involved in many metabolic processes. Seeking lower-cost and industrially scalable approaches for the synthesis of D-glutamine is very valuable both in academic career and potential applications. Herein, we developed a novel efficient chemoenzymatic strategy for producing D-glutamine. Initially, DL-glutamine was chemically prepared with cheap and accessible DL-glutamic acid as raw material. Subsequently, the L-glutamine among the racemic mixture was selectively hydrolyzed to L-glutamic acid by Escherichia coli whole-cell system which expressed L-aminopeptidase D-Ala-esterase/amidase (DmpA) from Ochrobactrum anthropi. The left D-glutamine was obtained by isoelectric point precipitation with 70% of the theoretical yield. Furthermore, we optimized enzymatic resolution conditions to determine the optimum parameters as pH 8, 30 °C, 0.1% (v/v) Triton X-100, and 1 mM Mn2+. These results suggested that our strategy might be potentially usable for the synthesis of D-glutamine in industrial productions.
Hydrolyzed metabolites of thalidomide: Synthesis and TNF-α production-inhibitory activity
Nakamura, Takanori,Noguchi, Tomomi,Miyachi, Hiroyuki,Hashimoto, Yuichi
, p. 651 - 654 (2008/02/08)
Putative hydrolyzed metabolites of thalidomide were prepared and characterized, and their inhibitory activity on tumor necrosis factor (TNF)-α production in the human monocytic leukemia cell line THP-1 was evaluated. α-(2-Carboxybenzamido)glutarimide was a more potent TNF-α production inhibitor than thalidomide.