Introduction: cholinesterases, from molecular complexity to non-hydrolytic functions

Proteins do not function alone, in an empty space; rather, their interchangeable interactions with other partner proteins have become a subject of intensive study in recent years. This inevitably raises several interesting questions, namely, do such interactions modify the initial features of the interacting proteins, and in what way(s)? This minireview series addresses the subject of protein–protein interactions and their effects on partner proteins and their cellular and tissue environment. It is focused on the long‐debated topic of whether the acetylcholine‐hydrolyzing enzyme, acetylcholinesterase (EC, has non‐hydrolytic functions, apart from and/or in addition to its enzymatic activities. The non‐hydrolytic functions of acetylcholinesterase have been the topic of a heated discussion ongoing in the cholinesterase community for several decades; recently, this discussion took the form of a dedicated session in the 2007 Cholinesterase meeting in Suzhou, China. Based on the arguments presented in that session, four different researchers were invited to provide their views on this question for the benefit of FEBS Journal readers, in the form of minireviews. The minireview series thus covers many different studies, based on distinct and unrelated experimental approaches, which together form a coherent body of information…

Authors: Soreq H.
Year of publication: 2008
Journal: FEBS J. 2008 Feb;275(4):603. Epub 2008 Jan 17.

Link to publication:


“Working memory”