PURIFICATION AND CHARACTERIZATION OF A BACTERIAL DEHALOGENASE WITH ACTIVITY TOWARD HALOGENATED ALKANES, ALCOHOLS AND ETHERS
PURIFICATION AND CHARACTERIZATION OF A BACTERIAL DEHALOGENASE WITH ACTIVITY TOWARD HALOGENATED ALKANES, ALCOHOLS AND ETHERS
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DOI：
10.1111/j.1432-1033.1988.tb13759.x
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发表时间：
1988-01-15
期刊：
影响因子：
--
通讯作者：
WITHOLT, B
中科院分区：
文献类型：
--
作者：
JANSSEN, DB;GERRITSE, J;WITHOLT, B
An enzyme that is capable of hydrolytic coversion 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 28000. 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 dihalomehtanes, C5 - C9 1-halo-n-alkanes, secondary alkylhalides, halogenatd alcohols and chlorinated ethers. Several of these compounds are important enviroment 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.
