As one answerer pointed out, the haloalkane dehalogenases are part of a/b hydrolase family, and as far as I know are limited to the bacterial realm. However, this is not to say that there is not a mammalian enzyme which could be 'recruited' to perform this reaction, as the haloalkane dehalogenases are homologous to other hydrolases which may have a mammalian counterpart. Even though mammalian Haloalkane dehalogenases may not exist, a P450 enzyme may be able to conduct the same reaction, but by an oxidative mechanism. So, for example, there are P450 enzymes (hydrocarbon utilizing yeast comes to mind) that will convert a 1-halo-alkane to the corresponding alcohol. Although the product would suggest a hydrolytic reaction, the biochemicstry is oxidative since O2 and NADH are required. You could easily test your substrate for a mammalian based P450 based dehalogenating reaction by using a liver homogenate, and supplyitng the required NADH + O2 to the reaction. Because of the complexity of the extract, and the likelihood of side reactions, I would follow the reaction by looking for the alcohol product (LC or GC), and not risk a colorimetric assay. Good luch

As fas as I know, related to that activity, in human beings I only have data on iodotyrosine dehalogenase. But CYP450 shows a lot of different activities ans capacities, so that the former suggestion by Dr. Karimi (assay with homogenated liver) is a reasonable idea to test. Pehaps you have preliminary results about it....

Good luck

There are no homologs of the bacterial alpha/beta-hydrolase family of haloalkane dehalogenases in humans that I am aware of.

It would be the easiest to measure if you could detect the halide released by the suspected dehalogenase. See Keuning S, Janssen DB, Witholt B. Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. J Bacteriol. 1985 Aug;163(2):635-9, and articles citing this article, for the assay. The halide assay is chromogenic, halides like chloride and bromide will result in a red color. You would probably have some background of the halides present in your liver homogenate. To detect disappearance of the halogenated substrate and release of the alcohol product you probably need GC if it is a small hydrophobic molecule that you are working with.

As one answerer pointed out, the haloalkane dehalogenases are part of a/b hydrolase family, and as far as I know are limited to the bacterial realm. However, this is not to say that there is not a mammalian enzyme which could be 'recruited' to perform this reaction, as the haloalkane dehalogenases are homologous to other hydrolases which may have a mammalian counterpart. Even though mammalian Haloalkane dehalogenases may not exist, a P450 enzyme may be able to conduct the same reaction, but by an oxidative mechanism. So, for example, there are P450 enzymes (hydrocarbon utilizing yeast comes to mind) that will convert a 1-halo-alkane to the corresponding alcohol. Although the product would suggest a hydrolytic reaction, the biochemicstry is oxidative since O2 and NADH are required. You could easily test your substrate for a mammalian based P450 based dehalogenating reaction by using a liver homogenate, and supplyitng the required NADH + O2 to the reaction. Because of the complexity of the extract, and the likelihood of side reactions, I would follow the reaction by looking for the alcohol product (LC or GC), and not risk a colorimetric assay. Good luch