KAT I Inhibitors

KAT I Inhibitors constitutes a diverse group of compounds that share the ability to inhibit the activity of lysine acetyltransferase I. These inhibitors function through various mechanisms, such as direct competition with the enzyme's natural substrates, binding to the active site of the enzyme to impede its proper conformational dynamics, or mimicking the structure of coenzymes to disrupt the enzyme's normal activity. Some of these compounds, like anacardic acid and garcinol, are naturally occurring substances found in plant sources that have been found to possess inhibitory activity against KAT I. Others, such as C646 and I-CBP112, are synthetic molecules specifically designed to target the enzyme's acetyltransferase activity or its associated domains. Inhibitors such as curcumin and chrysin not only compete with substrates but may also induce conformational changes in KAT I that result in reduced enzymatic activity. Compounds like EGCG and quercetin, common in dietary sources, inhibit KAT I and have been extensively studied for their broader biological effects. Meanwhile, small molecules like MB-3 and BIX-01294 were developed through medicinal chemistry efforts to mimic or antagonize the structure and function of KAT I's natural substrates or associated proteins. Isoliquiritigenin and plumbagin represent additional classes of natural compounds that have been shown to exhibit inhibitory activity against KAT I through competitive inhibition or modulation of the enzyme's redox state.