PHOSPHOENOLPYRUVATE CARBOXYKINASE, FROM E COLI

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。PCK在糖异生中起关键作用。在Mg和ATP饱和条件下，PCK被Ca激活6倍，被Mn激活4倍。胰蛋白酶对PCK的消化导致25%的c端断裂。胰蛋白酶消化的PCK或截断的PCK失去了被Ca激活的能力；然而Mn的活化仍然存在。发现截断的PCK通过添加Ca重新获得2倍的激活。为了清楚地了解Ca和Mn对PCK的激活，以及如何恢复Ca的激活，我们结晶了四种独特的截断的PCK复合物。人们相信，截断的PCK晶体结构的知识可能有助于糖尿病的治疗。具体来说，人们认为PCK抑制剂有一天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.