This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Poelarends, G. J.
Right arrow Articles by Janssen, D. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Poelarends, G. J.
Right arrow Articles by Janssen, D. B.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 1999, p. 2050-2058, Vol. 181, No. 7
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Degradation of 1,2-Dibromoethane by Mycobacterium sp. Strain GP1

Gerrit J. Poelarends,1 Johan E. T. van Hylckama Vlieg,1 Julian R. Marchesi,2 Luisa M. Freitas Dos Santos,3,dagger and Dick B. Janssen1,*

Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands,1 and School of Pure and Applied Biology, University of Wales College of Cardiff, Cardiff CF1 3TL,2 and Department of Chemical Engineering and Chemical Technology, Imperial College, London SW7 2BY,3 United Kingdom

Received 23 September 1998/Accepted 18 January 1999

The newly isolated bacterial strain GP1 can utilize 1,2-dibromoethane as the sole carbon and energy source. On the basis of 16S rRNA gene sequence analysis, the organism was identified as a member of the subgroup which contains the fast-growing mycobacteria. The first step in 1,2-dibromoethane metabolism is catalyzed by a hydrolytic haloalkane dehalogenase. The resulting 2-bromoethanol is rapidly converted to ethylene oxide by a haloalcohol dehalogenase, in this way preventing the accumulation of 2-bromoethanol and 2-bromoacetaldehyde as toxic intermediates. Ethylene oxide can serve as a growth substrate for strain GP1, but the pathway(s) by which it is further metabolized is still unclear. Strain GP1 can also utilize 1-chloropropane, 1-bromopropane, 2-bromoethanol, and 2-chloroethanol as growth substrates. 2-Chloroethanol and 2-bromoethanol are metabolized via ethylene oxide, which for both haloalcohols is a novel way to remove the halide without going through the corresponding acetaldehyde intermediate. The haloalkane dehalogenase gene was cloned and sequenced. The dehalogenase (DhaAf) encoded by this gene is identical to the haloalkane dehalogenase (DhaA) of Rhodococcus rhodochrous NCIMB 13064, except for three amino acid substitutions and a 14-amino-acid extension at the C terminus. Alignments of the complete dehalogenase gene region of strain GP1 with DNA sequences in different databases showed that a large part of a dhaA gene region, which is also present in R. rhodochrous NCIMB 13064, was fused to a fragment of a haloalcohol dehalogenase gene that was identical to the last 42 nucleotides of the hheB gene found in Corynebacterium sp. strain N-1074.


* Corresponding author. Mailing address: Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands. Phone: 31-50-3634209. Fax: 31-50-3634165. E-mail: d.b.janssen{at}chem.rug.nl.

dagger Present address: SmithKline Beecham, Tonbridge TN11 9AN, Kent, United Kingdom.


Journal of Bacteriology, April 1999, p. 2050-2058, Vol. 181, No. 7
0021-9193/99/$04.00+0
Copyright © 1999, 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]  
  • Coleman, N. V., Spain, J. C. (2003). Epoxyalkane:Coenzyme M Transferase in the Ethene and Vinyl Chloride Biodegradation Pathways of Mycobacterium Strain JS60. J. Bacteriol. 185: 5536-5545 [Abstract] [Full Text]  
  • Marchesi, J. R., Weightman, A. J. (2003). Comparing the Dehalogenase Gene Pool in Cultivated {alpha}-Halocarboxylic Acid-Degrading Bacteria with the Environmental Metagene Pool. Appl. Environ. Microbiol. 69: 4375-4382 [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]  
  • Bosma, T., Damborsky, J., Stucki, G., Janssen, D. B. (2002). Biodegradation of 1,2,3-Trichloropropane through Directed Evolution and Heterologous Expression of a Haloalkane Dehalogenase Gene. Appl. Environ. Microbiol. 68: 3582-3587 [Abstract] [Full Text]  
  • van Hylckama Vlieg, J. E. T., Tang, L., Lutje Spelberg, J. H., Smilda, T., Poelarends, G. J., Bosma, T., van Merode, A. E. J., Fraaije, M. W., Janssen, D. B. (2001). Halohydrin Dehalogenases Are Structurally and Mechanistically Related to Short-Chain Dehydrogenases/Reductases. J. Bacteriol. 183: 5058-5066 [Abstract] [Full Text]  
  • Poelarends, G. J., Saunier, R., Janssen, D. B. (2001). trans-3-Chloroacrylic Acid Dehalogenase from Pseudomonas pavonaceae 170 Shares Structural and Mechanistic Similarities with 4-Oxalocrotonate Tautomerase. J. Bacteriol. 183: 4269-4277 [Abstract] [Full Text]  
  • Poelarends, G. J., Zandstra, M., Bosma, T., Kulakov, L. A., Larkin, M. J., Marchesi, J. R., Weightman, A. J., Janssen, D. B. (2000). Haloalkane-Utilizing Rhodococcus Strains Isolated from Geographically Distinct Locations Possess a Highly Conserved Gene Cluster Encoding Haloalkane Catabolism. J. Bacteriol. 182: 2725-2731 [Abstract] [Full Text]  
  • Poelarends, G. J., Kulakov, L. A., Larkin, M. J., van Hylckama Vlieg, J. E. T., Janssen, D. B. (2000). Roles of Horizontal Gene Transfer and Gene Integration in Evolution of 1,3-Dichloropropene- and 1,2-Dibromoethane-Degradative Pathways. J. Bacteriol. 182: 2191-2199 [Abstract] [Full Text]  
  • Damborsky, J., Koca, J. (1999). Analysis of the reaction mechanism and substrate specificity of haloalkane dehalogenases by sequential and structural comparisons. Protein Eng Des Sel 12: 989-998 [Abstract] [Full Text]  
  • Bosma, T., Kruizinga, E., de Bruin, E. J., Poelarends, G. J., Janssen, D. B. (1999). Utilization of Trihalogenated Propanes by Agrobacterium radiobacter AD1 through Heterologous Expression of the Haloalkane Dehalogenase from Rhodococcus sp. Strain m15-3. Appl. Environ. Microbiol. 65: 4575-4581 [Abstract] [Full Text]