Family Report for: Haloalkane_dehalogenase-HLD2
Haloalkane_dehalogenase-HLD2 | Rank | 2 |
| Family | Epoxide-hydrolase_like |
| Gene_locus (72) |
| Block | X |
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| Wikipedia | Haloalkane_dehalogenase |
| Paper (26) |
| Structure (130) |
| EC_number | 3.8.1.5 |
| Interpro | IPR023594 Haloalkane dehalogenase, subfamily 2 |
| 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. Although 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. Luciferase from Renilla reniformis (RLuc) catalyzes the degradation of coelenterazine in the presence of molecular oxygen, resulting in the product coelenteramide, carbon dioxide, and the desired photon of light (EC 1.13.12.5). This enzyme belongs to the Haloalkane dehalogenase family II with a different catalytic function (EC 3.8.1.5) (this luciferase is different from fireflies luciferases classified as Luciferin 4-monooxygenase; ATP-dependent AMP-binding enzyme family). Reconstruction of an ancestral enzyme shows it has both hydrolase and monooxygenase activities ( Chaloupkova et al.) |
| Pfam | PF00561 Abhydrolase_1 |
| Inhibitor (30) |
| Substrate (35) |
| Chemical | Isopropanol |
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