| 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)." |