缺乏鸟嘌呤-黄嘌呤磷酸核糖基转移酶的大肠杆菌突变体。
Escherichia coli mutants deficient in guanine-xanthine phosphoribosyltransferase.
作者信息
Holden J A, Harriman P D, Wall J D
出版信息
J Bacteriol. 1976 Jun;126(3):1141-8. doi: 10.1128/jb.126.3.1141-1148.1976.
Abstract
We studied the purine phosphoribosyltransferases (PRTases) of Escherichia coli and were able to isolate a mutant that is defective in its ability to convert guanine and xanthine to their respective ribonucleotides. The affected gene (gpt) lies between metD and proA and is 78.6% co-transducible with proA. Both this point mutant and a strain with a pro-lac deletion contain less than 2% of wild-type xanthine PRTase activity, yet still contain about 30% of wild-type guanine PRTase activity. Thus, the gpt gene is only one of at least two genes responsible for guanine PRTase activity in E. coli.
摘要
我们研究了大肠杆菌的嘌呤磷酸核糖转移酶（PRTases），并成功分离出一个突变体，该突变体在将鸟嘌呤和黄嘌呤转化为各自核糖核苷酸的能力上存在缺陷。受影响的基因（gpt）位于metD和proA之间，与proA的共转导率为78.6%。这个点突变体和一个pro-lac缺失菌株的黄嘌呤PRTase活性均不到野生型的2%，但仍含有约30%的野生型鸟嘌呤PRTase活性。因此，gpt基因只是大肠杆菌中至少两个负责鸟嘌呤PRTase活性的基因之一。
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