L-lactyl-CoA (precursor of the L-lactyl moiety) and S-D-lactylglutathione (precursor of the D-lactyl moiety), which enable enzymatic and non-enzymatic mechanisms of lysine lactylation, respectively. Initially found on histone proteins (e.g., H3K9, H3K18, H3K56, H4K8, H4K12), it is now known to also modify non-histone proteins like metabolic enzymes and transcription factors.

It plays a pivotal role in transcriptional activation and regulates protein function, stability, and cellular interactions.

The modification can be added via an enzymatic pathway (using L-lactyl-CoA) or a non-enzymatic pathway (using S-D-lactylglutathione). While specific regulatory enzymes are unknown, existing acetyltransferases and deacetylases are likely involved.

Lysine lactylation influences critical pathways in malignant transformation and metastasis, making it a promising new target for cancer therapy.