The influence of maltoporin affinity on the transport of maltose and maltohexaose into Escherichia coli.
The kinetics of maltose transport and its inhibition by maltohexaose were investigated using Escherichia coli strains with engineered modifications of maltoporin. The permeation of lactose through maltoporin was also measured, as well as its inhibition by maltohexaose. Based on these results, the role of the maltoporin binding site in transport was evaluated.
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D001665:Binding Sites; D001692:Biological Transport / Q000187:drug effects; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D004926:Escherichia coli / Q000378:metabolism* / Q000648:ultrastructure; D007785:Lactose / Q000378:metabolism; D008320:Maltose / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism*; D011134:Polysaccharides / Q000378:metabolism; D018272:Porins; D011991:Receptors, Virus / Q000378:metabolism*; D013379:Substrate Specificity
D001425:Bacterial Outer Membrane Proteins; D009844:Oligosaccharides; D011134:Polysaccharides; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins; C016549:maltohexaose; D008320:Maltose; C008315:maltodextrin; D007785:Lactose