title: l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1.
abstract: l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1 is a stereospecific enzyme that acts exclusively on l-isomers of 2-chloropropionate and dichloroacetate. The amino acid sequence of this enzyme is substantially different from those of other l-specific dehalogenases produced by other organisms. DehL has not been crystallised, and hence its three-dimensional structure is unavailable. Herein, we review what is known concerning DehL and tentatively identify the amino acid residues important for catalysis based on a comparative structural and sequence analysis with well-characterised l-specific dehalogenases.
authors.affiliation: Department of Biotechnology and Medical Engineering, Faculty of Biosciences and Medical Engineering, Universiti Teknologi Malaysia, 81310 Johor Baharu, Johor Malaysia.
authors.forename: Aliyu
authors.initials: A
authors.lastname: Adamu
authors.affiliation: Department of Chemistry, Faculty of Science, Universiti Teknologi Malaysia, 81310 Johor Baharu, Johor Malaysia.
authors.forename: Roswanira Abdul
authors.initials: RA
authors.lastname: Wahab
authors.affiliation: Department of Biotechnology and Medical Engineering, Faculty of Biosciences and Medical Engineering, Universiti Teknologi Malaysia, 81310 Johor Baharu, Johor Malaysia.
authors.forename: Fahrul
authors.identifier: 0000-0003-3978-4087
authors.initials: F
authors.lastname: Huyop
keywords: Catalytic amino acid residues; DehL; Dehalogenation; Rhizobium sp. RC1