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Identification of a eukaryotic reductive dechlorinase and characterization of its mechanism of action on its natural substrate.
- Source :
-
Chemistry & biology [Chem Biol] 2011 Oct 28; Vol. 18 (10), pp. 1252-60. - Publication Year :
- 2011
-
Abstract
- Chlorinated compounds are important environmental pollutants whose biodegradation may be limited by inefficient dechlorinating enzymes. Dictyostelium amoebae produce a chlorinated alkyl phenone called DIF which induces stalk cell differentiation during their multicellular development. Here we describe the identification of DIF dechlorinase. DIF dechlorinase is active when expressed in bacteria, and activity is lost from Dictyostelium cells when its gene, drcA, is knocked out. It has a K(m) for DIF of 88 nM and K(cat) of 6.7 s(-1). DrcA is related to glutathione S-transferases, but with a key asparagine-to-cysteine substitution in the catalytic pocket. When this change is reversed, the enzyme reverts to a glutathione S-transferase, thus suggesting a catalytic mechanism. DrcA offers new possibilities for the rational design of bioremediation strategies.<br /> (Copyright © 2011 Elsevier Ltd. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Amino Acid Substitution
Asparagine
Base Sequence
Catalytic Domain
Conserved Sequence
Cysteine
Gene Knockout Techniques
Glutathione metabolism
Glutathione Transferase metabolism
Hexanes metabolism
Kinetics
Lyases genetics
Molecular Sequence Data
Oxidoreductases
Protozoan Proteins genetics
Protozoan Proteins metabolism
Substrate Specificity
Dictyostelium enzymology
Hexanones metabolism
Hydrocarbons, Chlorinated metabolism
Lyases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1879-1301
- Volume :
- 18
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Chemistry & biology
- Publication Type :
- Academic Journal
- Accession number :
- 22035794
- Full Text :
- https://doi.org/10.1016/j.chembiol.2011.08.003