Study of Adenine Aminohydrolase in the Yeast, Schizosaccharomyces pombe

Author:

Abbondandolo Angelo1,Weyer Anne1,Heslot Henri1,Lambert Micheline1

Affiliation:

1. Department of Genetics, Institut National Agronomique, Paris, France

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference9 articles.

1. Adenine uptake and pool formation in the fission yeast Schizosaccharomyces pombe;Cummins J. E.;Biochim. Biophys. Acta,1967

2. Reg,ilation of adenylate deaminase by adenosine triphosphate;Cunningham B.;Biochim. Biophys. Acta,1965

3. La specificite des pyrophosphorylases des nucleotides puriques chez le Schizosaccharomyces pombe;De Groodt A.;C. R. Acad. Sci. Paris,1969

4. Adenine aminohydrolase. An investigation of specificity;Hartenstein R. C.;J. Biol. Chem.,1967

5. Purine catabolism in Drosophila melanogaster I. Reactions leading to xanthine dehydrogenase;Hodge L. D.;Biochim. Biophys. Acta,1967

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