Affiliations 

  • 1 Department of Biotechnology and Medical Engineering, Faculty of Biosciences and Medical Engineering, Universiti Teknologi Malaysia, 81310 Johor Baharu, Johor Malaysia
  • 2 Department of Chemistry, Faculty of Science, Universiti Teknologi Malaysia, 81310 Johor Baharu, Johor Malaysia
Springerplus, 2016;5(1):695.
PMID: 27347470 DOI: 10.1186/s40064-016-2328-9

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.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.