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• W1837172466 startingPage "635" @default.
• W1837172466 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." @default.
• W1837172466 created "2016-06-24" @default.
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• W1837172466 date "1985-08-01" @default.
• W1837172466 modified "2023-10-16" @default.
• W1837172466 title "Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10" @default.
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• W1837172466 doi "https://doi.org/10.1128/jb.163.2.635-639.1985" @default.
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