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Structure and Function of Cholinesterases from Agnathans and Cephalochordates

Implications for the Evolution of Cholinesterases

  • Chapter
Structure and Function of Cholinesterases and Related Proteins

Abstract

Jawed vertebrates possess two related cholinesterases (ChE’s), acetylcholinesterase (AChE, EC 3.1.1.7) and butyrylcholinesterase (BuChE, EC 3.1.1.8). AChE hydrolyzes acetylcholine at cholinergic synapses. The function of BuChE is unknown, but is suggested to play a role in growth and development, and to act as a scavenger of cholinergic toxins (1). The two ChE’s are distinguished on the basis of substrate specificity: AChE hydrolyzes acetylcholine and is virtually inactive on the larger substrate butyrylcholine. BuChE is less selective, hydrolyzing both substrates comparably. AChE exhibits substrate inhibition while BuChE does not, but may show substrate activation instead (2). The two enzymes are also distinguished by their susceptibility to diagnostic inhibitors (1).

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Pezzementi, L. et al. (1998). Structure and Function of Cholinesterases from Agnathans and Cephalochordates. In: Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. (eds) Structure and Function of Cholinesterases and Related Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1540-5_15

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  • DOI: https://doi.org/10.1007/978-1-4899-1540-5_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4899-1542-9

  • Online ISBN: 978-1-4899-1540-5

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