Maltose and maltodextrin utilization by Bacillus subtilis

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 UCB (MalP; synonym, GlvC), with an apparent K m of 5 μM and a Vmax of 91 nmol · min -1 · (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 V max of 4.7 nmol · min-1 · (1010 CFU)-1. Copyright © 2006, American Society for Microbiology. All Rights Reserved.