Abbondandolo A, Weyer A, Heslot H, Lambert M
J Bacteriol. 1971 Dec;108(3):959-63. doi: 10.1128/jb.108.3.959-963.1971.
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.
对粟酒裂殖酵母的一些无腺嘌呤突变体在六种取代嘌呤类似物上生长情况的观察，得出这样一个假说：存在一种酶，它催化这些类似物转化为次黄嘌呤。已发现腺嘌呤酶（腺嘌呤氨基水解酶，EC 3.5.4.2）在粟酒裂殖酵母的无细胞提取物中具有活性。报告的结果与该酶负责6-氯嘌呤在体内利用的假说相符。这一证据主要来自对两个在6-氯嘌呤上部分生长能力缺失的突变体中腺嘌呤氨基水解酶的研究。
