Previous Article | Next Article 
Applied and Environmental Microbiology, January 2000, p. 219-222, Vol. 66, No. 1
Department of Environmental Chemistry and
Ecotoxicology1 and Laboratory of
Biomolecular Structure and Dynamics,3 Masaryk
University, Kotlá
Received 3 June 1999/Accepted 18 October 1999
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 of 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 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, Mycobacterium avium MU1 and
Mycobacterium smegmatis CCM 4622, showed broad substrate specificity toward 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 colonizing both
animal tissues and free environment, indicates a possible role of
parasitic microorganisms in the distribution of degradation genes in
the environment.
0099-2240/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Dehalogenation of Haloalkanes by
Mycobacterium tuberculosis H37Rv and Other
Mycobacteria
ek,2 and
í
Damborský3,*
ská 2, 611 37 Brno, and
Czech Collection of Microorganisms, Tvrdého 14, 602 00 Brno,2 Czech Republic
*
Corresponding author. Mailing address: Laboratory of
Biomolecular Structure and Dynamics, Masaryk University,
Kotláská 2, 611 37 Brno, Czech Republic. Phone:
420-5-41129377. Fax: 420-5-41129506. E-mail:
jiri{at}chemi.muni.cz.
Applied and Environmental Microbiology, January 2000, p. 219-222, Vol. 66, No. 1
0099-2240/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
This article has been cited by other articles:
-
Jesenska, A., Pavlova, M., Strouhal, M., Chaloupkova, R., Tesinska, I., Monincova, M., Prokop, Z., Bartos, M., Pavlik, I., Rychlik, I., Mobius, P., Nagata, Y., Damborsky, J.
(2005). Cloning, Biochemical Properties, and Distribution of Mycobacterial Haloalkane Dehalogenases. Appl. Environ. Microbiol.
71: 6736-6745
[Abstract] [Full Text] -
Sato, Y., Monincova, M., Chaloupkova, R., Prokop, Z., Ohtsubo, Y., Minamisawa, K., Tsuda, M., Damborsky, J., Nagata, Y.
(2005). Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, Encode Haloalkane Dehalogenases with Novel Structures and Substrate Specificities. Appl. Environ. Microbiol.
71: 4372-4379
[Abstract] [Full Text] -
Nagata, Y., Prokop, Z., Marvanova, S., Sykorova, J., Monincova, M., Tsuda, M., Damborsky, J.
(2003). Reconstruction of Mycobacterial Dehalogenase Rv2579 by Cumulative Mutagenesis of Haloalkane Dehalogenase LinB. Appl. Environ. Microbiol.
69: 2349-2355
[Abstract] [Full Text] -
Jesenska, A., Bartos, M., Czernekova, V., Rychlik, I., Pavlik, I., Damborsky, J.
(2002). Cloning and Expression of the Haloalkane Dehalogenase Gene dhmA from Mycobacterium avium N85 and Preliminary Characterization of DhmA. Appl. Environ. Microbiol.
68: 3724-3730
[Abstract] [Full Text]
Copyright © 2010 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»