V-ATPases are membrane-embedded protein complexes that function as ATP hydrolysis-driven proton pumps. V-ATPases are the primary source of organellar acidification in all eukaryotes, making them essential for many fundamental cellular processes. Enzymatic activity can be modulated by regulated and reversible disassembly of the complex, and several subunits of mammalian V-ATPase have multiple isoforms that are differentially localized. Although the biochemical properties of the different isoforms are currently unknown, mutations in specific subunit isoforms have been associated with various diseases, making V-ATPases potential drug targets. V-ATPase structure and activity have been best characterized in Saccharomyces cerevisiae, where recent structures have revealed details about the dynamics of the enzyme, the proton translocation pathway, and conformational changes associated with regulated disassembly and autoinhibition.

中文翻译：

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V型ATP酶的结构和作用。

V-ATPases是膜嵌入的蛋白质复合物，起ATP水解驱动质子泵的作用。V-ATPase是所有真核生物中细胞器酸化的主要来源，使其成为许多基本细胞过程所必需的。酶的活性可以通过复合物的调节和可逆拆卸来调节，并且哺乳动物V-ATPase的几个亚基具有差异化定位的多个同工型。尽管目前尚不清楚不同同工型的生化特性，但特定亚基同工型的突变已与多种疾病相关，这使得V-ATPases成为潜在的药物靶标。V-ATPase的结构和活性在酿酒酵母中得到了最好的表征，其中最近的结构揭示了有关该酶动力学，质子转运途径，