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Literature DB >> 11466294

Specificity and topology of the Escherichia coli xanthosine permease, a representative of the NHS subfamily of the major facilitator superfamily.

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.

Entities: Chemical Gene Species

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Year: 2001 PMID： 11466294 PMCID： PMC99545 DOI： 10.1128/JB.183.16.4900-4904.2001

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

16 in total

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11 in total

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Authors: Sergio A Bucarey; Nicolás A Villagra; Mara P Martinic; A Nicole Trombert; Carlos A Santiviago; Nancy P Maulén; Philip Youderian; Guido C Mora
Journal: Infect Immun Date: 2005-10 Impact factor: 3.441

2. Xanthosine utilization in Salmonella enterica serovar Typhimurium is recovered by a single aspartate-to-glycine substitution in xanthosine phosphorylase.

Authors: Michael Riis Hansen; Jesper Tranekjaer Jørgensen; Gert Dandanell
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Authors: Sergio A Bucarey; Nicolas A Villagra; Juan A Fuentes; Guido C Mora
Journal: Genetics Date: 2006-02-19 Impact factor: 4.562