Purification and characterization of a bacterial dehalogenase with activity toward halogenated alkanes, alcohols and ethers
| Autor: | Christiaan Kalk, Bernard Witholt, Dick Jager, Josephine C. Brackman, Jan Gerritse, Dick B. Janssen |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1988 |
| Předmět: |
Hydrocarbons
Halogenated Hydrolases Chemistry Halogenation Stereoisomerism Ether Biochemistry Dibromomethane Substrate Specificity Catalysis Molecular Weight Kinetics chemistry.chemical_compound Asymmetric carbon Alcohols Actinomycetales Alkanes Nucleophilic substitution Organic chemistry Ethers Dehalogenase |
| Zdroj: | European Journal of Biochemistry, 171(1-2), 67-72. Blackwell Publishing Ltd |
| ISSN: | 0014-2956 |
| Popis: | An enzyme that is capable of hydrolytic conversion of halogenated aliphatic hydrocarbons to their corresponding alcohols was purified from a 1,6-dichlorohexane-degrading bacterium. The dehalogenase was found to be a monomeric protein of relative molecular mass 28,000. The affinity for its substrates was relatively low with Km values for short-chain haloalkanes in the range 0.1-0.9 mM. The aliphatic dehalogenase showed a much broader substrate range than has been reported for halidohydrolases so far. Novel classes of substrates include dihalomethanes, C5-C9 1-halo-n-alkanes, secondary alkylhalides, halogenated alcohols and chlorinated ethers. Several of these compounds are important environmental pollutants, e.g. methylbromide, dibromomethane, 1,2-dibromoethane, 1,3-dichloropropene, and bis(2-chloroethyl)ether. The degradation of chiral 2-bromoalkanes appeared to proceed without stereochemical preference. Optically active 2-bromobutane was converted with inversion of configuration at the chiral carbon atom, suggesting that the dehalogenase reaction proceeds by a nucleophilic substitution involving a carboxyl group or base catalysis. |
| Databáze: | OpenAIRE |
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