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Study of adenine aminohydrolase in the yeast, Schizosaccharomyces pombe.

Journal of Bacteriology, 01 Dec 1971, 108(3):959-963
https://doi.org/10.1128/jb.108.3.959-963.1971 PMID: 5139537 PMCID: PMC247174

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Abstract 

Observation of the growth of some adenineless mutants of Schizosaccharomyces pombe on six substituted purine analogs leads to the hypothesis that an enzyme is present which catalyzes the conversion of these analogs into hypoxanthine. The enzyme adenase (adenine aminohydrolase, EC 3.5.4.2) has been found to be active in cell-free extracts of S. pombe. Results are reported which are in agreement with the hypothesis that this enzyme is responsible for the in vivo utilization of 6-chloropurine. This evidence comes mainly from a study of adenine aminohydrolase in two mutants selected for partial inability to grow on 6-chloropurine.

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J Bacteriol. 1971 Dec; 108(3): 959–963.
PMCID: PMC247174
PMID: 5139537

Study of Adenine Aminohydrolase in the Yeast, Schizosaccharomyces pombe

Angelo Abbondandolo,1 Anne Weyer,2 Henri Heslot, and Micheline Lambert
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Abstract

Observation of the growth of some adenineless mutants of Schizosaccharomyces pombe on six substituted purine analogs leads to the hypothesis that an enzyme is present which catalyzes the conversion of these analogs into hypoxanthine. The enzyme adenase (adenine aminohydrolase, EC 3.5.4.2) has been found to be active in cell-free extracts of S. pombe. Results are reported which are in agreement with the hypothesis that this enzyme is responsible for the in vivo utilization of 6-chloropurine. This evidence comes mainly from a study of adenine aminohydrolase in two mutants selected for partial inability to grow on 6-chloropurine.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Cummins JE, Mitchison JM. Adenine uptake and pool formation in the fission yeast Schizosaccharomyces pombe. Biochim Biophys Acta. 1967 Feb 7;136(1):108–120. [Abstract] [Google Scholar]
  • CUNNINGHAM B, LOWENSTEIN JM. REGULATION OF ADENYLATE DEAMINASE BY ADENOSINE TRIPHOSPHATE. Biochim Biophys Acta. 1965 Mar 22;96:535–537. [Abstract] [Google Scholar]
  • Hartenstein RC, Fridovich I. Adenine aminohydrolase. An investigation of specificity. J Biol Chem. 1967 Feb 25;242(4):740–746. [Abstract] [Google Scholar]
  • Hodge LD, Glassman E. Purine catabolism in Drosophila melanogaster. I. Reactions leading to xanthine dehydrogenase. Biochim Biophys Acta. 1967 Dec 19;149(2):335–343. [Abstract] [Google Scholar]
  • LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [Abstract] [Google Scholar]
  • Rao SN, Hara L, Askari A. Alkali cation-activated AMP deaminase of erythrocytes: some properties of the membrane-bound enzyme. Biochim Biophys Acta. 1968 Mar 25;151(3):651–654. [Abstract] [Google Scholar]
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