• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>Proceedings of the National Academy of Sciences of the United States of America >Mechanism of negative cooperativity in glyceraldehyde-3-phosphate dehydrogenase deduced from ligand competition experiments.
【2h】

Mechanism of negative cooperativity in glyceraldehyde-3-phosphate dehydrogenase deduced from ligand competition experiments.

机译：由配体竞争实验推导的3-磷酸甘油醛脱氢酶中负协同作用的机理。

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

It is shown that the modulation in the negative cooperativity of ligand binding by another, competing ligand that binds noncooperatively is accounted for exclusively by the ligand-induced sequential model. It is therefore suggested that whenever such a phenomenon is observed it argues strongly in favor of the sequential model. The advantages and limitations of this approach are evaluated. The binding of the coenzymes NAD+ and nicotinamide-1-N6-ethenoadenine dinucleotide to rabbit muscle apo-glyceraldehyde-3-phosphate dehydrogenase [D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating; EC 1.2.1.12] exhibits strong negative cooperativity, whereas acetylpyridine adenine dinucleotide, ATP, and ADP-ribose bind noncooperatively to the NAD+ sites. The strong abolished in the presence of acetylpyridine adenine dinucleotide and strongly weakened by ATP, ADP, and AMP, but was not affected by addition of ADP-ribose. These findings demonstrate that the negative cooperativity in coenzyme binding to this enzyme results from sequential conformational changes and exclude the pre-existent asymmetry model as a possible explanation. These results also support the view that the structure of the pyridine moiety of the coenzyme analogs plays a role in orienting the adenine moiety at the adenine subsite, therefore affecting the cooperativity in the binding of the coenzyme analog which is mediated through the adenine subsites.
机译：结果表明，配体诱导的顺序模型仅解释了另一种非竞争性结合的竞争配体与配体结合的负协同作用的调节。因此建议，只要观察到这种现象，就强烈支持顺序模型。评估了这种方法的优点和局限性。辅酶NAD +和烟酰胺-1-N6-乙炔腺嘌呤二核苷酸与兔肌肉脱磷酸甘油醛-3-磷酸脱氢酶[D-甘油醛-3-磷酸：NAD +氧化还原酶（磷酸化； EC 1.2.1.12）的结合）具有很强的负协同性，乙酰吡啶腺嘌呤二核苷酸，ATP和ADP-核糖与NAD +位点不合作结合，在乙酰吡啶腺嘌呤二核苷酸存在下被强力消除，而被ATP，ADP和AMP强烈减弱，但不受添加ADP-核糖的影响。这些发现表明，辅酶与该酶结合的负协同作用是由于连续的构象变化引起的，并且排除了可能存在的不对称模型，这些结果也支持了辅酶类似物的吡啶部分结构起着一定的作用。在将腺嘌呤部分定位于腺嘌呤亚位点时发挥作用，因此影响辅酶类似物结合中的协同作用这是通过腺嘌呤亚位点介导的。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号