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Structural Distinctions among Acetylcholinesterase Forms

  • Chapter
The Enzymes of Biological Membranes

Abstract

Acetylcholinesterase (EC 3.1.1.7) is associated primarily with cells involved in cholinergic synaptic transmission, but it is also found in a variety of other neuronal and a few nonneuronal cells, like erythrocytes, in which its function is unclear (Nachmansohn, 1959). The catalytic properties of acetylcholinesterase have been studied intensively for more than 40 years, and details about its specificity and catalytic mechanism and features that distinguish it from the similar enzyme cholinesterase (EC 3.1.1.8) can be found in many reviews (Froede and Wilson, 1971; Rosenberry, 1975; Massoulié and Bon, 1982). Although no role in synaptic transmission for cholinesterase has yet been demonstrated, it is remarkable that both these enzymes exist in multiple forms with striking structural parallels (see Massoulié and Bon, 1982). This review will focus on the protein structures of various acetylcholinesterase forms and on the relationship of these structures to cellular localization.

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  1. Department of Pharmacology, Case Western Reserve University, Cleveland, Ohio, 44106, USA

    Terrone L. Rosenberry

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  1. State University of New York, Syracuse, New York, USA

    Anthony N. Martonosi

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© 1985 Plenum Press, New York

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Rosenberry, T.L. (1985). Structural Distinctions among Acetylcholinesterase Forms. In: Martonosi, A.N. (eds) The Enzymes of Biological Membranes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4601-2_11

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  • DOI: https://doi.org/10.1007/978-1-4684-4601-2_11

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-4603-6

  • Online ISBN: 978-1-4684-4601-2

  • eBook Packages: Springer Book Archive

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