Stavrianopoulos J G, Chargaff E
Biochim Biophys Acta. 1981 Oct 27;655(3):307-22. doi: 10.1016/0005-2787(81)90040-x.
A previously described synthetase system of Escherichia coli that utilizes ribonucleoside triphosphates has been purified extensively and shown to consist of an apoenzyme and three protein factors. The apoenzyme itself was revealed to be polynucleotide phosphorylase. The conditions under which the latter - an enzyme incorporating nucleoside diphosphates - is converted to a system catalyzing the uptake of nucleoside triphosphates have been studied in detail with respect to primer requirements, the influence of triphosphates on diphosphate utilization and vice versa, and the possibly regulatory effect of the guanosine di- and triphosphates. The fully supplemented enzyme system (polynucleotide synthetase) incorporates GTP only in the presence of ATP, producing a polynucleotide with an A : G ratio near unity.
先前描述的利用核糖核苷三磷酸的大肠杆菌合成酶系统已被广泛纯化,并显示由一种脱辅酶和三种蛋白质因子组成。脱辅酶本身被发现是多核苷酸磷酸化酶。关于引物需求、三磷酸对二磷酸利用的影响以及反之亦然,以及鸟苷二磷酸和三磷酸可能的调节作用,已经详细研究了将后者——一种掺入核苷二磷酸的酶——转化为催化核苷三磷酸摄取的系统的条件。完全补充的酶系统(多核苷酸合成酶)仅在ATP存在的情况下掺入GTP,产生A:G比接近1的多核苷酸。