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Journal of Bacteriology, June 2006, p. 3911-3922, Vol. 188, No. 11
0021-9193/06/$08.00+0 doi:10.1128/JB.00213-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Iris Andernach,
Gabriele Witz, and
Michael K. Dahl
Department of Biology, University of Konstanz, D-78457 Konstanz, Germany
Received 8 February 2006/ Accepted 15 March 2006
Bacillus subtilis can utilize maltose and maltodextrins that are derived from polysaccharides, like starch or glycogen. In this work, we show that maltose is taken up by a member of the phosphoenolpyruvate-dependent phosphotransferase system and maltodextrins are taken up by a maltodextrin-specific ABC transporter. Uptake of maltose by the phosphoenolpyruvate-dependent phosphotransferase system is mediated by maltose-specific enzyme IICB (MalP; synonym, GlvC), with an apparent Km of 5 µM and a Vmax of 91 nmol · min1 · (1010 CFU)1. The maltodextrin-specific ABC transporter is composed of the maltodextrin binding protein MdxE (formerly YvdG), with affinities in the low micromolar range for maltodextrins, and the membrane-spanning components MdxF and MdxG (formerly YvdH and YvdI, respectively), as well as the energizing ATPase MsmX. Maltotriose transport occurs with an apparent Km of 1.4 µM and a Vmax of 4.7 nmol · min1 · (1010 CFU)1.
Present address: Lehrstuhl für Mikrobiologie, Fachbereich Biologie/Chemie der Universität Osnabrück, D-49069 Osnabrück, Germany.
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