Acetylcholinesterase (AChE) hydrolysis rate

Range with acetylcholine (ACh) as substrate >10^8M^-1×sec^-1: with ACh analog acetylazacholine 4,000M^-1×s M^-1×sec^-1
Organism Unspecified
Reference Massoulié J, Pezzementi L, Bon S, Krejci E, Vallette FM. Molecular and cellular biology of cholinesterases. Prog Neurobiol. 1993 Jul41(1):31-91 p.53 left column 2nd paragraphPubMed ID8321908
Primary Source Quinn, D. M. (1987) Acetylcholinesterase: enzyme structure, reaction dynamics and virtual transition states. Chem. Rev. 87, 955-979 AND Quinn, D. M., Pryor, A. N., Selwood, T., Lee, B. H., Acheson, S. A. and Barlow, P. N. (1991) The chemical mechanism of acetylcholinesterase reactions. Biological catalysis at the speed limit. In: Cholinesterases: Structure, Function, Mechanism, Genetics and Cell Biology, pp. 252-257. Eds. J. Massoulie, F. Bacou, E. A. Barnard, A. Chatonnet, B. P. Doctor and D. M. Quinn. American Chemical Society: Washington D.C.
Comments P.53 left column 2nd paragraph: "AChE hydrolyzes a large variety of substrates, esters, thioesters, selenoesters, anilides, amides, with rates ranging over more than 5 orders of magnitude, e.g. as between acetylcholine (>10^8M^-1×sec^-1) and its amide analog acetylazacholine (4×10^3M^-1×sec^-1) (see primary sources). The active site of AChE appears to display some conformational adaptability (Rosenberry, 1975a)."
Entered by Uri M
ID 115060