PMID:11466294

Citation	Nørholm, MH and Dandanell, G (2001) Specificity and topology of the Escherichia coli xanthosine permease, a representative of the NHS subfamily of the major facilitator superfamily. J. Bacteriol. 183:4900-4
Abstract	The specificity of XapB permease was compared with that of the known nucleoside transporters NupG and NupC. XapB-mediated xanthosine uptake is abolished by 2,4-dinitrophenol and exhibits saturation kinetics with an apparent K(m) of 136 microM. A 12-transmembrane-segment model was confirmed by translational fusions to alkaline phosphatase and the alpha fragment of beta-galactosidase.
Links	PubMed PMC99545 Online version:10.1128/JB.183.16.4900-4904.2001
Keywords	Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins; Kinetics; Membrane Proteins/metabolism; Membrane Transport Proteins; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Ribonucleosides/metabolism; Software; Substrate Specificity
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