Recent progress in 2-haloacid dehalogenases.

Author: Yayue WANG ¹ ; Song XUE ² ; Qingfeng ZHOU ¹ ; Dongli PEI ¹
Author Information

1. College of Biology and Food, Shangqiu Normal University, Shangqiu 476000, Henan, China.
2. Laboratory of Biotechnology, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, Liaoning, China.
Publication Type:Journal Article
Keywords: 2-haloacid dehalogenases; application; catalytic mechanism; protein structure
MeSH: Catalysis; Halogenation; Hydrolases; chemistry; metabolism; Hydrolysis; Research; trends; Substrate Specificity
From: Chinese Journal of Biotechnology 2020;36(5):868-878
CountryChina
Language:Chinese
Abstract: 2-Haloacid dehalogenases (EC 3.8.1.X) catalyze the hydrolytic dehalogenation of 2-haloacids, releasing halogen ions and producing corresponding 2-hydroxyacids. The enzymes not only degrade xenobiotic halogenated pollutants, but also show wide substrate profile and astonishing efficiency for enantiomer resolution, making them valuable in environmental protection and the green synthesis of optically pure chiral compounds. A variety of 2-haloacid dehalogenases have been biochemically characterized so far. Further studies have been made in protein crystal structures and catalytic mechanisms. Here, we review the recent progresses of 2-haloacid dehalogenases in their source, protein structures, reaction mechanisms, catalytic properties and application. We also suggest further research directions for 2-haloacid dehalogenase.