Possible mechanisms of lysine acetylation and deacetylation.

Lysine acetyl-transferases (KATs), such as YfiQ, utilize acetyl-CoA (AcCoA) to donate an acetyl group to lysine. Lysine deacetylases (KDACs), such as CobB, can deacetylate some lysines in a NAD⁺-dependent manner. While other KDACs, such as YcgC, deacetylate in a NAD⁺-independent manner. Sequence alignments suggest that KATs and at least one KDAC may be present in N. gonorrhoeae. Non-enzymatic acetylation utilizes acetyl-phosphate (AcP), the high-energy intermediate in the Pta-AckA pathway, as the acetyl donor.