KAT2A (lysine acetyltransferase 2A) is a versatile chr17-modifying enzyme that functions as both a histone acetyltransferase and succinyltransferase/lactyltransferase, playing critical roles in gene regulation and cellular metabolism. As a histone acetyltransferase, KAT2A acetylates histone H3, particularly at lysine 9, to regulate transcription 1. Beyond acetylation, KAT2A exhibits dual enzymatic activities: it functions as a succinyltransferase when coupled with the α-ketoglutarate dehydrogenase complex, succinylating histone H3 at lysine 79 near transcription start sites to promote gene expression and tumor cell proliferation 2, and as a lactyltransferase when complexed with ACSS2, catalyzing histone lactylation that drives tumor immune evasion through Wnt/β-catenin, NF-κB, and PD-L1 expression 3. KAT2A is essential for intestinal stem cell maintenance, preventing double-stranded RNA accumulation and interferon signaling 4. In disease contexts, KAT2A represents a therapeutic target in acute myeloid leukemia, where its inhibition induces myeloid differentiation and apoptosis while sparing normal hematopoietic cells 5. The enzyme also contributes to breast cancer metastasis through interactions with methylated SNIP1 and c-MYC 6, and promotes macrophage polarization in septic lung injury via STAT1 succinylation 7.