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Applied and Environmental Microbiology, April 2003, p. 2349-2355, Vol. 69, No. 4
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.4.2349-2355.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Reconstruction of Mycobacterial Dehalogenase Rv2579 by Cumulative Mutagenesis of Haloalkane Dehalogenase LinB

Yuji Nagata,1* Zbynek Prokop,2 Sona Marvanová,2 Jana Sykorová,2 Marta Monincová,2 Masataka Tsuda,1 and Jirí Damborsky2

Department of Life Sciences, Graduate School of Life Sciences, Tohoku University, Sendai 980-8577, Japan,1 National Centre for Biomolecular Research, Masaryk University, 611 37 Brno, Czech Republic2

Received 3 September 2002/ Accepted 13 January 2003

The homology model of protein Rv2579 from Mycobacterium tuberculosis H37Rv was compared with the crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26, and this analysis revealed that 6 of 19 amino acid residues which form an active site and entrance tunnel are different in LinB and Rv2579. To characterize the effect of replacement of these six amino acid residues, mutations were introduced cumulatively into the six amino acid residues of LinB. The sixfold mutant, which was supposed to have the active site of Rv2579, exhibited haloalkane dehalogenase activity with the haloalkanes tested, confirming that Rv2579 is a member of the haloalkane dehalogenase protein family.

* Corresponding author. Mailing address: Department of Life Sciences, Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Sendai 980-8577, Japan. Phone: 81-22-217-5682. Fax: 81-22-217-5704. E-mail: aynaga{at}ige.tohoku.ac.jp.

Applied and Environmental Microbiology, April 2003, p. 2349-2355, Vol. 69, No. 4
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.4.2349-2355.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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