Abstract
The 2-haloacid dehalogenases (EC 3.8.1.X) are industrially important enzymes that catalyze the cleavage of carbon–halogen bonds in 2-haloalkanoic acids, releasing halogen ions and producing corresponding 2-hydroxyl acids. These enzymes are of particular interest in environmental remediation and environmentally friendly synthesis of optically pure chiral compounds due to their ability to degrade a wide range of halogenated compounds with astonishing efficiency for enantiomer resolution. The 2-haloacid dehalogenases have been extensively studied with regard to their biochemical characterization, protein crystal structures, and catalytic mechanisms. This paper comprehensively reviews the source of isolation, classification, protein structures, reaction mechanisms, biochemical properties, and application of 2-haloacid dehalogenases; current trends and avenues for further development have also been included.
Highlights
Halogenated organic compounds show excellent thermal conductivity, insulation, heat resistance, lipophilicity, and biological activity (Kim et al, 2020; Zakary et al, 2021)
The dehalogenation catalyzed by D-DEX is directly mediated by activated water molecules, without forming an ester intermediate in the reaction process; this is the same process as DL-DEXi (Figure 7B)
The 2-haloacid dehalogenases show typical stereoselectivity; little is known about the stereoselective mechanism
Summary
Halogenated organic compounds show excellent thermal conductivity, insulation, heat resistance, lipophilicity, and biological activity (Kim et al, 2020; Zakary et al, 2021). We review the isolation source, classification, molecular structure, catalytic mechanism, catalytic properties, and industrial applications of 2-haloacid dehalogenases. The 2-haloacid dehalogenases have been classified according to amino acid sequence conservation and substrate selectivity (Wang et al, 2018; Adamu et al, 2020).
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