1971
DOI: 10.1128/jb.108.3.959-963.1971
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Study of Adenine Aminohydrolase in the Yeast, Schizosaccharomyces pombe

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… Show more

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Cited by 10 publications
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“…Allam et al ( 1981 ) reported that ADE has only a natural substrate, adenine, but other studies showed that ADE can also hydrolyze 6-halogenpurines (Abbondandolo et al, 1971 ; Jun and Sakai, 1985 ). It was observed that Klac ADA is able to consume adenine, 2,6-diaminopurine, 6-chloropurine, and 8-azaguanine.…”
Section: Discussionmentioning
confidence: 99%
“…Allam et al ( 1981 ) reported that ADE has only a natural substrate, adenine, but other studies showed that ADE can also hydrolyze 6-halogenpurines (Abbondandolo et al, 1971 ; Jun and Sakai, 1985 ). It was observed that Klac ADA is able to consume adenine, 2,6-diaminopurine, 6-chloropurine, and 8-azaguanine.…”
Section: Discussionmentioning
confidence: 99%