Schlattner U, Forstner M, Eder M, Stachowiak O, Fritz-Wolf K, Wallimann T
Swiss Federal Institute of Technology, Institute of Cell Biology, ETH Zürich.
Mol Cell Biochem. 1998 Jul;184(1-2):125-40.
Mitochondrial creatine kinase (Mi-CK) is a central enzyme in energy metabolism of tissues with high and fluctuating energy requirements. In this review, recent progress in the functional and structural characterization of Mi-CK is summarized with special emphasis on the solved X-ray structure of chicken Mib-CK octamer (Fritz-Wolf et al., Nature 381, 341-345, 1996). The new results are discussed in a historical context and related to the characteristics of CK isoforms as known from a large number of biophysical and biochemical studies. Finally, two hypothetical functional aspects of the Mi-CK structure are proposed: (i) putative membrane binding motifs at the top and bottom faces of the octamer and (ii) a possible functional role of the central 20 A channel.
线粒体肌酸激酶(Mi-CK)是能量需求高且波动的组织能量代谢中的关键酶。在本综述中,总结了Mi-CK功能和结构表征方面的最新进展,特别强调了已解析的鸡Mib-CK八聚体的X射线结构(弗里茨 - 沃尔夫等人,《自然》381卷,341 - 345页,1996年)。在历史背景下讨论了这些新结果,并将其与大量生物物理和生化研究中已知的CK同工型特征相关联。最后,提出了Mi-CK结构的两个假设功能方面:(i)八聚体顶面和底面的假定膜结合基序,以及(ii)中央20埃通道可能的功能作用。