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Adenosine Accumulation in Saccharomyces Cerevisiae Cultured in Medium Containing Low Levels of Adenine

Overview
Journal J Bacteriol
Specialty Microbiology
Date 1986 Jun 1
PMID 3086289
Citations 3
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Abstract

By monitoring the in vivo incorporation of low concentrations of radiolabeled adenine into acid-soluble compounds, we observed the unusual accumulation of two nucleosides in Saccharomyces cerevisiae that were previously considered products of nucleotide degradation. Under the culture conditions used in the present study, radiolabeled adenosine was the major acid-soluble intracellular derivative, and radiolabeled inosine was initially detected as the second most prevalent derivative in a mutant lacking adenine aminohydrolase. The use of yeast mutants defective in the conversion of adenine to hypoxanthine or to AMP renders very unlikely the possibility that the presence of adenosine and inosine is attributable to nucleotide degradation. These data can be explained by postulating the existence of two enzyme activities not previously reported in S. cerevisiae. The first of these activities transfers ribose to the purine ring and may be attributable to purine nucleoside phosphorylase (EC 2.4.2.1) or adenosine phosphorylase (EC 2.4.2.-). The second enzyme converts adenosine to inosine and in all likelihood is adenosine aminohydrolase (EC 3.5.4.4).

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Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis.

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Deeley M J Bacteriol. 1992; 174(10):3102-10.

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References
1.
Minato S . Adenosine deaminase from takadiastase. V. Subunits of enzyme and interaction with adenosine analogues. J Biochem. 1968; 64(6):815-26. DOI: 10.1093/oxfordjournals.jbchem.a128964. View

2.
Kornberg A, Lieberman I, Simms E . Enzymatic synthesis of purine nucleotides. J Biol Chem. 1955; 215(1):417-27. View

3.
Martin Jr D, Gelfand E . Biochemistry of diseases of immunodevelopment. Annu Rev Biochem. 1981; 50:845-77. DOI: 10.1146/annurev.bi.50.070181.004213. View

4.
Korn E, Buchanan J . Biosynthesis of the purines. VI. Purification of liver nucleoside phosphorylase and demonstration of nucleoside synthesis from 4-amino-5-imidazolecarboxamide, adenine, and 2, 6-diaminopurine. J Biol Chem. 1955; 217(1):183-91. View

5.
Pickering W, Woods R . The uptake and incorporation of purines by wild-type Saccharomyces cerevisiae and a mutant resistant to 4-aminopyrazolo (3,4-d) pyrimidine. Biochim Biophys Acta. 1972; 264(1):45-58. DOI: 10.1016/0304-4165(72)90115-8. View