Uptake of AMP, ADP, and ATP inEscherichia coliW
| Autor: | Koichiro Isoi, Satsuki Tomioka, Kiyoko Tanimura, Kimiko Watanabe, Hisae Oku |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Adenosine monophosphate
Cytoplasm Adenylate kinase Purine nucleoside phosphorylase Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry chemistry.chemical_compound Adenosine Triphosphate Adenosine deaminase Nucleotidases Escherichia coli medicine Carbon Radioisotopes Inosine 5'-Nucleotidase Molecular Biology biology Adenine Nucleotides Organic Chemistry Biological Transport AMP deaminase General Medicine Molecular biology Adenosine Monophosphate Adenosine Diphosphate Adenosine diphosphate Purine-Nucleoside Phosphorylase chemistry Mutation Periplasm biology.protein Adenosine triphosphate Biotechnology medicine.drug |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 75:7-12 |
| ISSN: | 1347-6947 0916-8451 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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