Structure and Function of Cholinesterases from Agnathans and Cephalochordates

Implications for the Evolution of Cholinesterases
  • Leo Pezzementi
  • David Sutherland
  • Michael Sanders
  • Weily Soong
  • Daniel Milner
  • James Scott McClellan
  • Mathew Sapp
  • William Blake Coblentz
  • Gabriel Rulewicz
  • Sarah Merritt
Chapter

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).

Keywords

Bony Fish AChE Gene Peripheral Anionic Site Jawless Vertebrate Branchiostoma Lanceolatum 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Leo Pezzementi
    • 1
  • David Sutherland
    • 1
  • Michael Sanders
    • 1
  • Weily Soong
    • 1
  • Daniel Milner
    • 1
  • James Scott McClellan
    • 1
  • Mathew Sapp
    • 1
  • William Blake Coblentz
    • 1
  • Gabriel Rulewicz
    • 1
  • Sarah Merritt
    • 1
  1. 1.Division of Science and MathematicsBirmingham-Southern CollegeBirminghamUSA

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