Chao H M
J Biol Chem. 1976 Apr 25;251(8):2330-3.
A nucleoside phosphotransferase, which catalyzes the phosphorylation of nucleosides to nucleotides by low energy phosphate esters, has been isolated and purified 500-fold from the membrane fraction of Erwinia herbicola. Its most noteworthy difference from other enzymes of this class is that it is membrane bound and can be isolated and handled only in the presence of a detergent. With a ribonucleoside acceptor, adenosine, the reaction product is exclusively 5'-AMP; with deoxyadenosine, 5'- and 3'-nucleotide products appear in the approximate ratio of 2:1, respectively. The enzyme has no detectable phosphatase activity with the best phosphate donors, 5'-dAMP and 5'-dTMP, and very little with less active donors, such as p-nitrophenyl phosphate. This phosphotransferase should be a useful agent for preparing 5'-nucleotides from unusual synthetic bases.
一种核苷磷酸转移酶已从草生欧文氏菌的膜部分中分离并纯化了500倍，该酶通过低能磷酸酯催化核苷磷酸化为核苷酸。它与这类其他酶最显著的区别在于它与膜结合，并且只有在洗涤剂存在的情况下才能分离和处理。以核糖核苷受体腺苷为例，反应产物仅为5'-AMP；以脱氧腺苷为例，5'-和3'-核苷酸产物的出现比例分别约为2:1。该酶对最佳磷酸供体5'-dAMP和5'-dTMP没有可检测到的磷酸酶活性，对活性较低的供体如对硝基苯磷酸酯的活性也很小。这种磷酸转移酶应该是从非常规合成碱基制备5'-核苷酸的有用试剂。
