Comparison of Available Kinetic and Pharmacological Parameters and Splice Variants of Vertebrate AChE, BChE, and Atypical BChEs.

aData are from Toutant et al., [17]; the IC50 values are estimates.
bData are from Stieger et al. [19].
cData are from Lundin and represent titremetric measurement of the hydrolysis of the oxyesters rather than the thioesters of substrates [18].
dData are from Leibel and inhibition by BW284c51 is based on qualitative observations of the inhibition of ATCh staining of enzyme following non-denaturing gel electrophoresis [21]. Splice variant data are from Leibel [20].
eData are from Davies et al. [100].
fData are from Ucar et al. [101].
gData are from Loewenstein-Lichtenstein et al.; IC50 was back calculated from a calculated Ki[69].
hData are from Blong et al. [37].
iA, acetylthiocholine; P, propionylthiocholine; B, butyrylthiocholine; +, inhibition by high substrate concentrations; -, no inhibition; substrate activation is not considered.
jN.M., not measureable.
kN.D., not determined.
lSplice variant determined by molecular forms present and sequence data when available.