Similar to how plant peroxisomal enzymes bind propionyl-CoA and isobutyryl-CoA, Gen5, an acetyltransferase in humans, binds to propionyl-CoA and butyryl-CoA. These specifically bind to the catalytic domain of Gen5L2. This conserved acetyltransferase is responsible for the regulation of transcription by lysine acetylation of the histone N-terminal tails. This function of acetylation has a much higher reaction rate than propionylation or butyrylation. Because of the structure of propionyl-CoA, Gen5 distinguishes between different acyl-CoA molecules. In fact, it was found that the propyl group of butyrl-CoA cannot bind due to lack of stereospecificity to the active binding site of Gen5 due to the unsaturated acyl chains. On the other hand, the third carbon of propionyl-CoA can fit into the active site of Gen5 with the correct orientation.