5856-63-3Relevant articles and documents
Biochemical and Structural Characterization of an (R)-Selective Transaminase in the Asymmetric Synthesis of Chiral Hydroxy Amines
Li, Fulong,Liang, Youxiang,Wei, Yuwen,Zheng, Yukun,Du, Yan,Yu, Huimin
supporting information, p. 4582 - 4589 (2021/08/07)
An (R)-selective transaminase RbTA with excellent stereoselectivity (>99% ee) in the asymmetric amination of hydroxy ketones was identified. Biochemical characterization showed that RbTA exhibited the highest activity toward 4-hydroxy-2-butanone among reported enzymes, and that it has broad substrate specificity, including for aliphatic, aromatic, and alicyclic ketones. Crystallization of RbTA were performed, as were molecular docking and mutagenesis studies. Residue Tyr125 plays a key role in substrate recognition by forming a hydrogen bond with hydroxy ketone. The applicability of the enzyme was determined in preparative-scale synthesis of (R)-3-amino-1-butanol, demonstrating the potential of RbTA as a green biocatalyst for production of value-added chiral hydroxy amines. This study provides an efficient tool for enzymatic synthesis of chiral hydroxy amines, as well as structural insight into substrate recognition by transaminases in the asymmetric amination of hydroxy ketones. (Figure presented.).
Efficient continuous kinetic resolution of racemic 2-aminobutanol over immobilized penicillin G acylase
Wang, Jianxin,Liu, Na,Cheng, Xiaobo,Chen, Ligong
supporting information, p. 956 - 962 (2016/07/07)
In this paper, an efficient method was established for continuous kinetic resolution of racemic 2-aminobutanol by selective hydrolysis of N-phenylacetyl (±)-2-aminobutanol over immobilized penicillin G acylase (PGA) in a fixed-bed reactor. Several N-acylated derivatives of 2-aminobutanol were screened in batch experiments, and it was found that the hydrolysis of N-phenylacetyl (±)-2-aminobutanol proceeded smoothly in the presence of immobilized penicillin G acylase with satisfied enantioselectivity. Thus, the reaction parameters were optimized in a fixed-bed reactor. Under the optimized conditions, 39.3% conversion of N-phenylacetyl (±)-2-aminobutanol and 98.2% ee value of S-2-aminobutanol were obtained. This fixed-bed system was operated continuously for 40?h without significant decrease of enzyme activity. It has been demonstrated to be more efficient compared to the batch experiments.
Synthesis of imidacloprid derivatives with a chiral alkylated imidazolidine ring and evaluation of their insecticidal activity and affinity to the nicotinic acetylcholine receptor
Nishiwaki, Hisashi,Kuriyama, Mituhiro,Nagaoka, Hikaru,Kato, Akira,Yamauchi, Satoshi,Shuto, Yoshihiro,Akamatsu, Miki
, p. 6305 - 6312,8 (2012/12/11)
A series of imidacloprid (IMI) derivatives with an alkylated imidazolidine ring were asymmetrically synthesized to evaluate their insecticidal activity against adult female housefly, Musca domestica, and affinity to the nicotinic acetylcholine receptor of the flies. The bulkier the alkyl group, the lower was the receptor affinity, but the derivatives methylated and ethylated at the R-5-position of the imidazolidine ring were equipotent to the unsubstituted compound. Quantitative structure-activity relationship (QSAR) analysis of the receptor affinity demonstrated that the introduction of a substituent into the imidazolidine ring was fundamentally disadvantageous, but the introduction of a substituent at the R-5-position was permissible in the case of its small size. The binding model of the synthesized derivatives with the receptor supported the QSAR analysis, indicating the existence of space for a short alkyl group around the R-5-position in the ligand-binding site. In addition, positive correlation was observed between the insecticidal activity and receptor affinity, suggesting that the receptor affinity was the primary factor in influencing the insecticidal activity even if the imidazolidine ring was modified.
