Butyrylcholinesterase stimulation by homocysteine thiolactone linking vascular risk factors and Alzheimer's disease

The enzymatic activity of human butyrylcholinesterase is stimulated by homocysteine thiolactone. This stimulation results from the ability of homocysteine thiolactone and other primary unprotonated amine compounds to shift butyrylcholinesterase to its activated form. This stimulation does not result from an ability of these compounds to mimic substrate activation as this stimulation does not result from binding to the peripheral anionic site. Herein are discussed new kinetic equations for the modeling of this interaction between butyrylcholinesterase and homocysteine thiolactone. This stimulation may have vast implications in our understanding of arteriosclerosis and Alzheimer's disease.