大肠杆菌的多核苷酸合成酶:一种具有多核苷酸磷酸化酶作为脱酶的酶复合体

Jannis G. Stavrianopoulos , Erwin Chargaff
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引用次数: 0

摘要

先前描述的利用三磷酸核糖核苷的大肠杆菌合成酶系统已被广泛纯化,并显示由一种脱酶和三种蛋白质因子组成。该脱酶本身为多核苷酸磷酸化酶。后者——一种结合核苷二磷酸的酶——转化为催化核苷三磷酸吸收的系统的条件已经详细研究了引物要求,三磷酸对二磷酸利用的影响,反之亦然,鸟苷二磷酸和三磷酸可能的调节作用。充分补充的酶系统(多核苷酸合成酶)仅在ATP存在的情况下结合GTP,产生a: G比例接近统一的多核苷酸。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Polynucleotide synthetase of E. coli: An enzyme complex having polynucleotide phosphorylase as apoenzyme

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.

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