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Applied and Environmental Microbiology, August 2009, p. 5157-5160, Vol. 75, No. 15
0099-2240/09/$08.00+0 doi:10.1128/AEM.00199-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

a Koudeláková,1
Khomaini Hasan,1
Radka Chaloupková,1
Zbyn
k Prokop,1
Arie Geerlof,2 and
Ji
í Damborsk
1*
Loschmidt Laboratories, Institute of Experimental Biology and National Center for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5/A4, 625 00 Brno, Czech Republic,1 EMBL—Hamburg Outstation, DESY, Building 25A, Notkestraße 85, 22603 Hamburg, Germany2
Received 28 January 2009/ Accepted 30 May 2009
This study focuses on two representatives of experimentally uncharacterized haloalkane dehalogenases from the subfamily HLD-III. We report biochemical characterization of the expression products of haloalkane dehalogenase genes drbA from Rhodopirellula baltica SH1 and dmbC from Mycobacterium bovis 5033/66. The DrbA and DmbC enzymes show highly oligomeric structures and very low activities with typical substrates of haloalkane dehalogenases.
Published ahead of print on 5 June 2009.
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