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Updated: Jun 5, 2026

Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles
Published on: December 31, 2019
Uptake of AMP, ADP, and ATP in Escherichia coli W
Kimiko Watanabe1, Satsuki Tomioka, Kiyoko Tanimura
1School of Pharmacy and Pharmaceutical Sciences, Mukogawa Women's University, 11-68 Kyubancho, Koshien, Nishinomiya, Hyogo 633-8179, Japan. kimiko-watanabe@niche.tohoku.ac.jp
Abstract:
The uptake activity ratio for AMP, ADP, and ATP in mutant (T-1) cells of Escherichia coli W, deficient in de novo purine biosynthesis at a point between IMP and 5-aminoimidazole-4-carboxiamide-1-β-D-ribofuranoside (AICAR), was 1:0.43:0.19. This ratio was approximately equal to the 5'-nucleotidase activity ratio in E. coli W cells. The order of inhibitory effect on [2-³H]ADP uptake by T-1 cells was adenine > adenosine > AMP > ATP. About 2-fold more radioactive purine bases than purine nucleosides were detected in the cytoplasm after 5 min in an experiment with [8-¹⁴C]AMP and T-1 cells. Uptake of [2-³H]adenosine in T-1 cells was inhibited by inosine, but not in mutant (Ad-3) cells of E. coli W, which lacked adenosine deaminase and adenylosuccinate lyase. These experiments suggest that AMP, ADP, and ATP are converted mainly to adenine and hypoxanthine via adenosine and inosine before uptake into the cytoplasm by E. coli W cells.
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