title: Multi-template homology-based structural model of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1.
abstract: Dehalogenases are of high interest due to their potential applications in bioremediation and in synthesis of various industrial products. DehL is an L-2-haloacid dehalogenase (EC 3.8.1.2) that catalyses the cleavage of halide ion from L-2-halocarboxylic acid to produce D-2-hydroxycarboxylic acid. Although DehL utilises the same substrates as the other L-2-haloacid dehalogenases, its deduced amino acid sequence is substantially different (<25%) from those of the rest L-2-haloacid dehalogenases. To date, the 3D structure of DehL is not available. This limits the detailed understanding of the enzyme's reaction mechanism. The present work predicted the first homology-based model of DehL and defined its active site. The monomeric unit of the DehL constitutes α/β structure that is organised into two distinct structural domains: main and subdomains. Despite the sequence disparity between the DehL and other L-2-haloacid dehalogenases, its structural model share similar fold as the experimentally solved L-DEX and DehlB structures. The findings of the present work will play a crucial role in elucidating the molecular details of the DehL functional mechanism.
authors: a Faculty of Biosciences and Medical Engineering, Department of Biotechnology and Medical Engineering , Universiti Teknologi Malaysia , Johor Bahru 81310 , Johor , Malaysia.|c Faculty of Science, Department of Microbiology , Kaduna State University , Tafawa Balewa way, Kaduna PMB 2339 , Nigeria.
authors: Aliyu
authors: A
authors: Adamu
authors: a Faculty of Biosciences and Medical Engineering, Department of Biotechnology and Medical Engineering , Universiti Teknologi Malaysia , Johor Bahru 81310 , Johor , Malaysia.
authors: Mohd Shahir
authors: MS
authors: Shamsir
authors: b Faculty of Science, Department of Chemistry , Universiti Teknologi Malaysia , Johor Bahru 81310 , Johor , Malaysia.
authors: Roswanira Abdul
authors: http://orcid.org/0000-0002-9982-6587
authors: RA
authors: Wahab
authors: d Biotechnology Research Center , Tabriz University of Medical Sciences , Tabriz , Iran.
authors: Sepideh
authors: S
authors: Parvizpour
authors: a Faculty of Biosciences and Medical Engineering, Department of Biotechnology and Medical Engineering , Universiti Teknologi Malaysia , Johor Bahru 81310 , Johor , Malaysia.
authors: Fahrul
authors: F
authors: Huyop
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D017124:Conserved Sequence; D006867:Hydrolases / Q000737:chemistry*; D062105:Molecular Docking Simulation; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D012231:Rhizobium / Q000201:enzymology; D040681:Structural Homology, Protein; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D006867:Hydrolases; C034507:2-haloacid dehalogenase
keywords: DehL; Rhizobium sp RC1; dehalogenase; homology model