METAPHOSPHATE SYNTHESIS BY AN ENZYME FROM ESCHERICHIA-COLI

METAPHOSPHATE SYNTHESIS BY AN ENZYME FROM ESCHERICHIA-COLI
复制标题

DOI:
10.1016/0006-3002(56)90280-3
复制
发表时间:
1956-01-01
期刊:
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子:
--
通讯作者:
SIMMS, ES
SIMMS, ES
中科院分区:
其他
文献类型:
--
作者:
KORNBERG, A;KORNBERG, SR;SIMMS, ES

文献摘要

被引文献

相似文献

一种合成偏磷酸盐的酶从大肠杆菌提取物中纯化了 100 倍以上。该反应可用下式描述: [图片] 在聚合物中仅发现 ATP 的末端磷酸基团。由于该反应的另一种产物 ADP 被证明是一种非常有效的抑制剂,因此人们相信 ATP 再生系统通常与该反应偶联。无机焦磷酸盐(PP),但不是无机正磷酸盐或腺嘌呤核苷酸,被掺入偏磷酸盐中。然而,缺乏对 PP 的要求以及不存在 PP-ase 的任何抑制作用,使得真正的引物 (PO3)n 的性质受到怀疑。磷酸盐聚合物被称为长链偏磷酸盐,因为它(a)诱导异色性,(b)与蛋白质形成酸不溶性复合物,(c)不可透析,(d)对酸和碱不稳定,(e)与阴离子交换树脂牢固结合,并且(f)不受核酸酶攻击。
An enzyme that synthesizes metaphosphate was purified more than 100-fold from extracts of E. coli. The reaction may be described by the equation: [image] Only the terminal phosphate group of ATP was found in the polymer. Since ADP, the other product of the reaction, proved to be a very potent inhibitor, it is believed that an ATP-regen-erating system is generally coupled to the reaction. Inorganic pyrophosphate (PP), but not inorganic orthophosphate or adenine nucleotide, are incorporated into metaphosphate. However, lack of a requirement for PP and the absence of any inhibition by PP-ase leaves the nature of the true primer (PO3)n in doubt. The phosphate polymer is characterized as a long-chain metaphosphate because it (a) induces metachromasy, (b) forms an acid-insoluble complex with protein, (c) is nondialyzable, (d) is labile to acid and alkali, (e) binds tenaciously to anion exchange resins, and (f) is not attacked by nucleases.