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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

The slow rate of inhibition of acetylcholinesterase by fluoride.

We measured the rate of reaction of fluoride with acetylcholinesterase using a stopped flow apparatus for measurements on the millisecond time scale with phenylacetate as a chromogenic substrate. We found that the second order rate constant is 5 X 10(3) liters/ mol/sec, which is very slow for a small symmetric ion; it is 3-4 orders of magnitude smaller than for the substrates acetylcholine, acetylthiocholine, and phenylacetate. The slowness of this reaction suggests that fluoride does not find a preexisting binding site but must create one, probably by breaking and reforming hydrogen bonds. With hydrolysis measurements made on the usual time scale, we found kcat = 7.5 X 10(5) min-1 and KM = 2.0 mM. We also found that fluoride enhances substrate inhibition and that with low phenylacetate concentration the per cent inhibition is independent of substrate concentration.[1]


  1. The slow rate of inhibition of acetylcholinesterase by fluoride. Froede, H.C., Wilson, I.B. Mol. Pharmacol. (1985) [Pubmed]
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