Author:
Keuning S,Janssen D B,Witholt B
Abstract
A new enzyme, haloalkane dehalogenase, was isolated from the 1,2-dichloroethane-utilizing bacterium Xanthobacter autotrophicus GJ10. The purified enzyme catalyzed the hydrolytic dehalogenation of n-halogenated C1 to C4 alkanes, including chlorinated, brominated, and iodinated compounds. The highest activity was found with 1,2-dichloroethane, 1,3-dichloropropane, and 1,2-dibromoethane. The enzyme followed Michaelis-Menten kinetics, and the Km for 1,2-dichloroethane was 1.1 mM. Maximum activity was found at pH 8.2 and 37 degrees C. Thiol reagents such as p-chloromercuribenzoate and iodoacetamide rapidly inhibited the enzyme. The protein consists of a single polypeptide chain of a molecular weight of 36,000, and its amino acid composition and N-terminal sequence are given.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference28 articles.
1. The dehalogenases of 2,2-dichloropropionate degrading bacterium;Allison N.;Arch. Microbiol.,1983
2. Determination of trace amounts of chloride in naphtha;Bergmann J. G.;Anal. Chem.,1957
3. Bacterial degradation of dichloromethane;Brunner W.;Appl. Environ. Microbiol.,1980
4. The enzymatic cleavage of the carbonfluorine bond in fluoroacetate;Goldman P.;J. Biol. Chem.,1965
5. Carbon halogen bond cleavage. III. Studies on bacterial halidohydrolases;Goldman P.;J. Biol. Chem.,1968
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