Abstract
In vertebrates, acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are polymorphic enzymes presenting both globular and asymmetric forms1. In invertebrates, only AChE has been characterized so far that presents a reduced molecular diversity. In insects for example the major molecular form of AChE is an amphiphilic dimeric form2,3 attached to the membrane through a glycolipid covalently linked at the C-terminus of each catalytic subunit4,5,6. This AChE has a substrate specificity intermediate to those of mammalian AChE and BChE3,4. A glycolipid-anchored 7.5S form has also been observed in the trematode Schistosoma mansoni 7. Asymmetric forms have never been convincingly reported in invertebrates except in the more evolved animals such as Amphioxius 8. In the latter case also there is no BChE but AChE presents catalytic properties intermediate to those of vertebrate AChE and BChE8.
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© 1992 Springer Science+Business Media New York
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Arpagaus, M. et al. (1992). Nematode Acetylcholinesterases: Several Genes and Molecular Forms of Their Products. In: Shafferman, A., Velan, B. (eds) Multidisciplinary Approaches to Cholinesterase Functions. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3046-6_9
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DOI: https://doi.org/10.1007/978-1-4615-3046-6_9
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