| Literature DB >> 16707683 |
Stefan Schönert1, Sabine Seitz, Holger Krafft, Eva-Anne Feuerbaum, Iris Andernach, Gabriele Witz, Michael K Dahl.
Abstract
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 K(m) of 5 microM and a V(max) of 91 nmol . min(-1) . (10(10) 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 K(m) of 1.4 microM and a V(max) of 4.7 nmol . min(-1) . (10(10) CFU)(-1).Entities:
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Year: 2006 PMID: 16707683 PMCID: PMC1482931 DOI: 10.1128/JB.00213-06
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490