N-terminal acetylation (NTA) is one of the most widespread protein modifications, which occurs on most eukaryotic proteins, but is significantly less common on bacterial and archaea proteins. This modification is carried out by a family of enzymes called N-terminal acetyltransferases (NATs). To date, 12 NATs have been identified, harboring different composition, substrate specificity, and in some cases, modes of regulation. Recent structural and biochemical analysis of NAT proteins allows for a comparison of their molecular mechanisms and modes of regulation, which are described here. Although sharing an evolutionarily conserved fold and related catalytic mechanism, each catalytic subunit uses unique elements to mediate substrate-specific activity, and use NAT-type specific auxiliary and regulatory subunits, for their cellular functions.

N 端乙酰化 (NTA) 是最广泛的蛋白质修饰之一，它发生在大多数真核蛋白质上，但在细菌和古细菌蛋白质上明显不常见。这种修饰是由称为 N 端乙酰转移酶 (NAT) 的酶家族进行的。迄今为止，已经确定了 12 种 NAT，它们具有不同的组成、底物特异性，在某些情况下还具有调节模式。最近对 NAT 蛋白的结构和生化分析允许比较它们的分子机制和调节模式，这里描述。尽管共享进化上保守的折叠和相关的催化机制，但每个催化亚基都使用独特的元素来介导底物特异性活性，并使用 NAT 型特异性辅助和调节亚基来实现其细胞功能。