PHOSPHOENOLPYRUVATE CARBOXYKINASE, FROM E COLI

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。PCK在糖异生中起着关键作用。在镁和三磷酸腺苷饱和条件下，钙激活PCK 6倍，锰激活4倍。用胰酶消化PCK会导致25%的C末端被切割。胰酶消化PCK，或截短的PCK，失去了被钙激活的能力；但仍有锰的激活。截短的PCK被发现通过添加钙重新获得2倍的激活。为了更清楚地了解钙和锰对Pck的激活，以及如何恢复Ca的激活，我们结晶了四个独特的截断的Pck络合物。人们相信，了解截短的PCK的晶体结构可能有助于糖尿病的治疗。具体地说，人们认为PCK抑制剂有朝一日可能会减少对胰岛素的需求。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. PCK plays a critical role in gluconeogenesis. Under saturating conditions of Mg and ATP, PCK is activated 6 fold by the addition of Ca and 4 fold by Mn. Digestion of PCK by trypsin results in the cleavage of 25% of the C-terminus. Trypsin digested PCK, or truncated PCK, lost its ability to be activated by Ca; however Mn activation remained. Truncated PCK was found to reattain 2-fold activation by addition of Ca. In the hope of attaining a clear understanding of Pck activation by Ca and Mn, and how Ca activation can be regained four unique truncated Pck complexes were crystallized. It is believed knowledge of the crystal structure of truncated PCK may aid in the treatment of diabetes. Specifically it is believed a PCK inhibitor may one day reduced the need for insulin.