SUMMARYAcetylation is a conserved modification used to regulate a variety of cellular pathways, such as gene expression, protein synthesis, detoxification, and virulence. Acetyltransferase enzymes transfer an acetyl moiety, usually from acetyl coenzyme A (AcCoA), onto a target substrate, thereby modulating activity or stability. Members of the GCN5- N -acetyltransferase (GNAT) protein superfamily are found in all domains of life and are characterized by a core structural domain architecture. These enzymes can modify primary amines of small molecules or of lysyl residues of proteins. From the initial discovery of antibiotic acetylation, GNATs have been shown to modify a myriad of small-molecule substrates, including tRNAs, polyamines, cell wall components, and other toxins. This review focuses on the literature on small-molecule substrates of GNATs in bacteria, including structural examples, to understand ligand binding and catalysis. Understanding the plethora and versatility of substrates helps frame the role of acetylation within the larger context of bacterial cellular physiology.

中文翻译：

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在细菌中通过GCN5相关的N-乙酰转移酶进行小分子乙酰化。

概述乙酰化是一种保守的修饰，用于调节多种细胞途径，例如基因表达，蛋白质合成，排毒和毒力。乙酰基转移酶通常将乙酰基部分从乙酰辅酶A（AcCoA）转移到目标底物上，从而调节活性或稳定性。GCN5-N-乙酰基转移酶（GNAT）蛋白超家族成员存在于生活的所有域中，并具有核心结构域结构的特征。这些酶可以修饰小分子或蛋白质的赖氨酰残基的伯胺。从抗生素乙酰化的最初发现开始，已显示GNATs可以修饰无数的小分子底物，包括tRNA，多胺，细胞壁成分和其他毒素。这篇综述着重于细菌中GNAT的小分子底物的文献，包括结构实例，以了解配体结合和催化作用。了解底物的多样性和多功能性有助于在细菌细胞生理学的更大范围内阐明乙酰化的作用。