ENZYMOLOGICAL PROPERTIES OF POLY(ADP-RIBOSE) POLYMERASE - CHARACTERIZATION OF AUTOMODIFICATION SITES AND NADASE ACTIVITY
ENZYMOLOGICAL PROPERTIES OF POLY(ADP-RIBOSE) POLYMERASE - CHARACTERIZATION OF AUTOMODIFICATION SITES AND NADASE ACTIVITY
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DOI：
10.1016/0167-4838(91)99007-f
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发表时间：
1991-06-24
期刊：
影响因子：
--
通讯作者：
POIRIER, GG
中科院分区：
文献类型：
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作者：
DESMARAIS, Y;MENARD, L;POIRIER, GG
我们已经表征了聚（ADP-核糖）聚合酶自修饰对酶活性的影响，包括聚（ADP-核糖）合成和NAD酶活性。 在聚合物合成过程中，酶对NAD+的表观K（m）高于对交替NAD酶活性测量的K（m）。 此外，我们已经发现，有28个automodification网站，在15个网站（假设是在15个谷氨酸）报道存在于automodification域。 对于第一次，我们表明，这些受体位点的一些报告的automodification域（15 kDa）之外，我们证明了在NAD+结合域（55.2 kDa）和DNA结合域（42.5 kDa）的automodification。 我们分析了聚（ADP-核糖）聚合酶上修饰位点的数量与其对聚合活性的影响及其交替的NAD酶活性之间的关系。 自动修饰极大地改变了酶的活性，降低了聚合物的合成和交替的NAD酶活性。
We have characterized the effect of poly(ADP-ribose) polymerase automodification on the enzyme's activities, which include poly(ADP-ribose) synthesis and NADase activity. The apparent K(m) of the enzyme for NAD+ during polymer synthesis is higher than the one measured for alternate NADase activity. Furthermore, we have found that there are 28 automodification sites, in contrast to the 15 sites (postulated to be on the 15 glutamic acids) reported to be present in the automodification domain. For the first time, we show that some of these acceptor sites are outside the reported automodification domain (15 kDa); we demonstrate automodification in the NAD+ binding domain (55.2 kDa) and the DNA binding domain (42.5 kDa). We have analyzed the relationship between the number of sites modified on poly(ADP-ribose) polymerase and its effect on the polymerization activity and its alternate NADase activity. Automodification greatly altered both enzyme activities, decreasing both polymer synthesis and alternate NADase activity.