2-haloacid dehalogenase (2-HAD)

2-haloacid dehalogenase (EC 3.8.1.2) is a microbial enzyme that catalyzes the hydrolytic cleavage of carbon-halogen bonds in 2-haloalkanoic acids, converting them into 2-hydroxyalkanoic acids and halide ions (UniProt P22910). This enzyme is a key component in the biodegradation of halogenated organic compounds, such as chloroacetate and 2-chloropropionate, which are common environmental pollutants and components of certain herbicides (PubMed: 11473118). Based on their stereospecificity, these enzymes are categorized into L-specific, D-specific, and non-stereospecific types, each employing a nucleophilic substitution mechanism often involving a conserved aspartate residue (PubMed: 10480877). While 2-haloacid dehalogenases are not currently utilized as therapeutic targets for human disease, they are of significant interest in biotechnology for bioremediation and the industrial production of optically active chemicals. They belong to the broader Haloacid Dehalogenase-like (HAD) superfamily, which includes various phosphatases and hydrolases found across all domains of life, though the specific 2-haloacid dehalogenase activity is primarily associated with bacteria and archaea (BRENDA: EC 3.8.1.2).

Other names

L-2-haloacid dehalogenaseD-2-haloacid dehalogenase2-haloalkanoic acid dehalogenaseHaloacetate dehalogenaseDL-2-haloacid dehalogenase

Catalytic hydrolysis of carbon-halogen bonds via a nucleophilic substitution mechanism, typically involving a conserved aspartate residue that forms a covalent ester intermediate with the substrate.