In enzymology, a (R)-2-haloacid dehalogenase (), DL-2-haloacid halidohydrolase (inversion of configuration), DL-DEXi, (R,S)-2-haloacid dehalogenase (configuration-inverting)) is an enzyme that catalyzes the chemical reaction
(R)-2-haloacid + HO (S)-2-hydroxyacid + halide
Thus, the two substrates of this enzyme are (R)-2-haloacid and HO, whereas its two products are (S)-2-hydroxyacid and halide.
This enzyme belongs to the family of hydrolases, specifically those acting on halide bonds in carbon-halide compounds. The systematic name of this enzyme class is (R)-2-haloacid halidohydrolase. Other names in common use include 2-haloalkanoic acid dehalogenase[ambiguous], 2-haloalkanoid acid halidohydrolase[ambiguous], D-2-haloacid dehalogenase, and D-DEX.
D-DEXs lead to the production of 2-hydroxyacids and the release of halide ions from catalysing D-2-haloacid dehalogenation. D-DEXs are part of Group I dehalogenases, and this is due to similarity of the amino acid sequence. The D-DEX production of L-2-chloropropionic acid as an intermediate is related to herbicide production, there is a 30% similarity between DL-DEXs and D-DEXs in structure, and differences in DL-DEXs and D-DEXs are due to structural differences of the helical bend and the loop.
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