Dehalogenation of haloalkanes by Mycobacterium tuberculosis H37Rv and other mycobacteria
| Authors | |
|---|---|
| Year of publication | 2000 |
| Type | Article in Periodical |
| Magazine / Source | Applied and Environmental Microbiology |
| MU Faculty or unit | |
| Citation | |
| Web | http://www.ncbr.chemi.muni.cz/~jiri/ABSTRACTS/aem00.html |
| Field | Microbiology, virology |
| Keywords | holoalkane dehalogenases |
| Description | Haloalkane dehalogenases convert haloalkanes to their corresponding alcohols by a hydrolytic mechanism. To date various haloalkane dehalogenases have been isolated from bacteria colonizing environments that are contaminated with halogenated compounds. A search in current databases with the sequences of these known haloalkane dehalogenases revealed the presence of three different genes encoding putative haloalkane dehalogenases in the genome of the human parasite Mycobacterium tuberculosis strain H37Rv. The ability of M. tuberculosis and several other mycobacterial strains to dehalogenate haloaliphatic compounds was therefore studied. Intact cells of M. tuberculosis H37Rv were found to dehalogenate 1-chlorobutane, 1-chlorodecane, 1-bromobutane and 1,2-dibromoethane. Nine isolates of mycobacteria from clinical material and four strains from a collection of microorganisms were found to be capable of dehalogenating 1,2-dibromoethane. Crude extracts prepared from two of these strains, M. avium MU1 and M. smegmatis CCM 4622, showed broad substrate specificity towards a number of halogenated substrates. Dehalogenase activity in the absence of oxygen and the identification of primary alcohols as the products of the reaction suggest a hydrolytic dehalogenation mechanism. The presence of dehalogenases in bacterial isolates from clinical material including the species colonising both animal tissues and free environment indicates possible role of parasitic microorganisms in distribution of degradation genes in the environment. |
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