Department of Veterinary Medical Sciences, University of Bologna, Via Tolara di Sopra, 50, 40064, Ozzano Emilia, Bologna, Italy.
Biochimie. 2022 Jul;198:92-95. doi: 10.1016/j.biochi.2022.03.012. Epub 2022 Mar 30.
The FF-ATPase has Mg cofactor as the natural divalent cation to support the bifunctional activity of ATP synthesis and hydrolysis. Different physio(patho)logical conditions permit the molecular interaction of Ca with the enzyme and the modification of the biological role. Three distinct binding regions of Ca have been localized on the enzyme complex: one in the F catalytic sites and the other two sites in the membrane-embedded domain F. In all likelihood, Ca-activated enzyme most frequently works as an H-translocating FF-ATP(hydrol)ase with a monofunctional activity that triggers the formation of mitochondrial permeability transition pore (mPTP) phenomenon. The protein(s) component of the mPTP is considered an arcane mystery. However, the FF-ATPase could reveal the molecular mechanism of pore opening when Ca is bound to the enzyme. In this regard, the role of Ca-dependent function of the FF-ATPase in the formation of the mPTP is discussed.
FF-ATP 酶以镁辅因子作为天然二价阳离子来支持 ATP 合成和水解的双功能活性。不同的生理（病理）条件允许 Ca 与酶的分子相互作用，并改变其生物学作用。已经在酶复合物上定位了三个不同的 Ca 结合区域：一个在 F 催化部位，另外两个在膜嵌入的 F 域。很可能，Ca 激活的酶最常作为具有单功能活性的 H 转运 FF-ATP（水解）酶起作用，该活性触发线粒体通透性转换孔（mPTP）现象的形成。mPTP 的蛋白质（s）成分被认为是一个神秘的谜团。然而，当 Ca 结合到酶上时，FF-ATP 酶可以揭示孔打开的分子机制。在这方面，讨论了 Ca 依赖性 FF-ATP 酶功能在 mPTP 形成中的作用。
