The zinc-dependent histone deacetylases (HDACs 1–11) belong to the arginase-deacetylase superfamily of proteins, members of which share a common α/β fold and catalytic metal binding site. While several HDACs play a role in epigenetic regulation by catalyzing acetyllysine hydrolysis in histone proteins, the biological activities of HDACs extend far beyond histones. HDACs also deacetylate nonhistone proteins in the nucleus as well as the cytosol to regulate myriad cellular processes. The substrate pool is even more diverse in that certain HDACs can hydrolyze other covalent modifications. For example, HDAC6 is also a lysine decrotonylase, and HDAC11 is a lysine-fatty acid deacylase. Surprisingly, HDAC10 is not a lysine deacetylase but instead is a polyamine deacetylase. Thus, the HDACs are biologically and chemically versatile catalysts as they regulate the function of diverse protein and nonprotein substrates throughout the cell.

中文翻译：

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IIb 类组蛋白脱乙酰酶催化和抑制中的化学多功能性

锌依赖性组蛋白脱乙酰酶 (HDAC 1-11) 属于精氨酸酶-脱乙酰酶蛋白超家族，其成员具有共同的 α/β 折叠和催化金属结合位点。虽然多种 HDAC 通过催化组蛋白中的乙酰赖氨酸水解在表观遗传调控中发挥作用，但 HDAC 的生物活性远远超出了组蛋白的范围。 HDAC 还使细胞核和细胞质中的非组蛋白去乙酰化，以调节多种细胞过程。底物池更加多样化，因为某些 HDAC 可以水解其他共价修饰。例如，HDAC6也是赖氨酸去巴豆酰化酶，HDAC11是赖氨酸脂肪酸脱酰酶。令人惊讶的是，HDAC10 不是赖氨酸脱乙酰酶，而是多胺脱乙酰酶。因此，HDAC 是生物学和化学上通用的催化剂，因为它们调节整个细胞中多种蛋白质和非蛋白质底物的功能。