Enzymes
UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline xanthosine Identifier CHEBI:18107 (CAS: 146-80-5) help_outline Charge 0 Formula C10H12N4O6 InChIKeyhelp_outline UBORTCNDUKBEOP-UUOKFMHZSA-N SMILEShelp_outline OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c1[nH]c(=O)[nH]c2=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,836 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:28939 | RHEA:28940 | RHEA:28941 | RHEA:28942 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Specificity and topology of the Escherichia coli xanthosine permease, a representative of the NHS subfamily of the major facilitator superfamily.
Noerholm M.H., Dandanell G.
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 tran ... >> More
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. << Less