Fröhlich K U, Fries H W, Peters J M, Mecke D
Physiologisch-chemisches Institut, Tübingen, Germany.
Biochim Biophys Acta. 1995 Nov 15;1253(1):25-32. doi: 10.1016/0167-4838(95)00136-i.
The cell cycle protein CDC48p from Saccharomyces cerevisiae is a member of a protein superfamily (AAA superfamily) characterized by a common region of approximately 200 amino-acid residues including an ATP binding consensus. CDC48p purified to homogeneity showed considerable ATPase activity which could be completely abolished by preincubation with NEM in the absence of ATP. ATP protects the protein from NEM and stabilizes the otherwise labile enzyme. The ATPase activity is reversibly inhibited by NADH and shows cooperativity with its substrate ATP. The application of the in vitro ATPase activity to the identification of physiologically interacting molecules is discussed. By electron microscopy, the enzyme was shown to consist of hexameric ring structures similar to its vertebrate homologue.
来自酿酒酵母的细胞周期蛋白CDC48p是一个蛋白质超家族（AAA超家族）的成员，其特征是有一个约200个氨基酸残基的共同区域，包括一个ATP结合共有序列。纯化至同质的CDC48p显示出相当可观的ATP酶活性，在无ATP的情况下与NEM预孵育可使其完全丧失。ATP可保护该蛋白免受NEM影响，并稳定原本不稳定的酶。NADH可可逆地抑制ATP酶活性，且该酶对其底物ATP表现出协同性。本文讨论了体外ATP酶活性在鉴定生理相互作用分子方面的应用。通过电子显微镜观察，该酶显示为由类似于其脊椎动物同源物的六聚体环状结构组成。
