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Updated: Mar 18, 2026
A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments
Published on: October 2, 2012
l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1
Aliyu Adamu1, Roswanira Abdul Wahab2, Fahrul Huyop1
1Department of Biotechnology and Medical Engineering, Faculty of Biosciences and Medical Engineering, Universiti Teknologi Malaysia, 81310 Johor Baharu, Johor Malaysia.
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.
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