Reversible histone acylation is crucial for epigenetic gene expression regulation. Histone acylation is typically mediated by lysine acyltransferases (KATs), which use acyl-CoAs as acyl donors. Here, we revealed the novel role of the histone deacetylases HDAC1 and HDAC2 in histone acylation catalysis. Notably, we show that HDAC1 and HDAC2 directly catalyze sorbylation using sorbic acid, a common food preservative, in addition to facilitating desorbylation. This newly discovered HDAC1/2-driven histone sorbylation function is a distinctive active epigenetic mark that leads to widespread changes in the expression of genes, particularly those involved in cholesterol biosynthesis. Our findings reveal that HDAC1/2 are unique enzymes capable of catalyzing not only the removal but also formation of histone modifications in response to exogenous carboxylic acids such as sorbic acid and benzoic acid. Our results highlight the impact of carboxylic acids found in the environment, such as food additives, on gene expression changes that occur via histone lysine modification regulated by HDAC1 and HDAC2.