Haloacid dehalogenases of Rhizobium sp. and related enzymes: Catalytic properties and mechanistic analysis

Abstract

Haloacid dehalogenases catalyse the cleavage of carbon − halogen bonds in halogenated organic acids. These enzymes are of high interest due to their potential applications in bioremediation and in synthesis of various industrial products. The efficiency of dehalogenases in various applications can be enhanced, provided that their molecular catalytic mechanisms are fully understood. Herein, we review the current understanding of enzymatic haloacid dehalogenation mechanisms and the important amino acid residues that are necessary for the enzyme’s catalysis, with special emphasis on haloacid dehalogenases produced by Rhizobium sp.