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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.

SUBMITTER: Adamu A 

PROVIDER: S-EPMC4899344 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

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l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1.

Adamu Aliyu A   Wahab Roswanira Abdul RA   Huyop Fahrul F  

SpringerPlus 20160520 1


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 fo  ...[more]

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