Haloalkane_dehalogenase-HLD1

Family: Haloalkane_dehalogenase-HLD1

Block: X

Parent Family: Epoxide-hydrolase_like

Comment

Haloalkane dehalogenases (HLDs) are enzymes that catalyze the cleavage of carbon halogen bonds by a hydrolytic mechanism. The catalytic triad consists of the key nucleophile (Asp) the general base (His) and a catalytic acid (Asp or Glu). HLD where subdivided in three subfamily (Chovancova et al.) according to their substrate specificity and position of active site residues. Class one HLD1 (HLD-I) has catalytic triad Asp-His-Asp and halide-strabilizing residues Trp-Trp. Class two HLDII (HLD-II) has catalytic triad Asp-His-Glu and halide-stabilizing residues Asn-Trp. Class three HLDIII (HLD-III) has catalytic triad Asp-His-Asp and halide-strabilizing residues Asn-Trp. Also the reaction performed is different, the Renilla reniformis luciferase belongs to this family. In ESTHER as in HAMAP database class I and III are merged as they are close. OleB from bacterial hydrocarbon biosynthesis is a beta-lactone decarboxylase (Christenson et al.)