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 Monincová, M.
Right arrow Articles by Damborsky, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Monincová, M.
Right arrow Articles by Damborsky, J.
Agricola
Right arrow Articles by Monincová, M.
Right arrow Articles by Damborsky, J.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, March 2007, p. 2005-2008, Vol. 73, No. 6
0099-2240/07/$08.00+0     doi:10.1128/AEM.02416-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Weak Activity of Haloalkane Dehalogenase LinB with 1,2,3-Trichloropropane Revealed by X-Ray Crystallography and Microcalorimetry{triangledown}

Marta Monincová,1 Zbynek Prokop,1 Jitka Vévodová,2 Yuji Nagata,3 and Jirí Damborsky1*

Loschmidt Laboratories, Faculty of Science, Masaryk University, Kamenice 5/A4, 625 00 Brno, Czech Republic,1 Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW, United Kingdom,2 Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, Sendai, 2-1-1 Katahira, Sendai 980-8577, Japan3

Received 13 October 2006/ Accepted 18 January 2007

1,2,3-Trichloropropane (TCP) is a highly toxic and recalcitrant compound. Haloalkane dehalogenases are bacterial enzymes that catalyze the cleavage of a carbon-halogen bond in a wide range of organic halogenated compounds. Haloalkane dehalogenase LinB from Sphingobium japonicum UT26 has, for a long time, been considered inactive with TCP, since the reaction cannot be easily detected by conventional analytical methods. Here we demonstrate detection of the weak activity (kcat = 0.005 s–1) of LinB with TCP using X-ray crystallography and microcalorimetry. This observation makes LinB a useful starting material for the development of a new biocatalyst toward TCP by protein engineering. Microcalorimetry is proposed to be a universal method for the detection of weak enzymatic activities. Detection of these activities is becoming increasingly important for engineering novel biocatalysts using the scaffolds of proteins with promiscuous activities.

* Corresponding author. Mailing address: Loschmidt Laboratories, Masaryk University, Kamenice 5/A4, 625 00 Brno, Czech Republic. Phone: 420-5-4949 3467. Fax: 420-5-4949 2556. E-mail: jiri{at}chemi.muni.cz.

{triangledown} Published ahead of print on 26 January 2007.

Applied and Environmental Microbiology, March 2007, p. 2005-2008, Vol. 73, No. 6
0099-2240/07/$08.00+0     doi:10.1128/AEM.02416-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Jesenska, A., Monincova, M., Koudelakova, T., Hasan, K., Chaloupkova, R., Prokop, Z., Geerlof, A., Damborsky, J. (2009). Biochemical Characterization of Haloalkane Dehalogenases DrbA and DmbC, Representatives of a Novel Subfamily. Appl. Environ. Microbiol. 75: 5157-5160 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»