| Literature DB >> 1089626 |
Abstract
Adenosine 5'-monophosphate is dephosphorylated before its uptake by cells of Escherichia coli. This is demonstrated by using a radioactive double-labeled culture, and with a 5'-nucleotidase-deficient, mutant strain. The adenosine formed is further phosphorolyzed to adenine as a prerequisite for its uptake and incorporation. The cellular localization of the enzymes involved in the catabolism of adenosine 5'-monophosphate is discussed.Entities:
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Year: 1975 PMID: 1089626 PMCID: PMC245943 DOI: 10.1128/jb.121.2.401-405.1975
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490