Article
Binding modes of DL-2-haloacid dehalogenase revealed by crystallography, modeling and isotope effects studies.
Archives of biochemistry and biophysics - 1 Dec 2013
Siwek Agata, Omi Rie, Hirotsu Ken, Jitsumori Keiji, Esaki Nobuyoshi, Kurihara Tatsuo, Paneth Piotr
Abstract excerpt
Several pathways of biotic dechlorination can be found in enzymes, each characterized by different chlorine isotopic fractionation, which can thus serve as a signature of a particular mechanism. Unlike other dehalogenases, DL-2-haloacid dehalogenase, DL-DEX, converts both enantiomers of the substrate. Chlorine isotope effects for this enzyme are larger than in the case of other dehalogenases. Recently, the 3D...
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