| Title : Acetylcholinesterase: how is structure related to function? - Silman_2008_Chem.Biol.Interact_175_3 |
| Author(s) : Silman I , Sussman JL |
| Ref : Chemico-Biological Interactions , 175 :3 , 2008 |
|
Abstract :
In accordance with its biological role, termination of neurotransmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter, acetylcholine, acetylcholinesterase is one of nature's most efficient enzymes. Solution of its three-dimensional structure revealed that its active site is located at the bottom of a deep and narrow gorge. Such an architecture was unanticipated in view of its high turnover number. The present review examines how the highly specialized structure of acetylcholinesterase, with its sequestered active site, contributes to its catalytic efficacy, and discusses how the traffic of substrate and products to and from the active site is controlled. |
| PubMedSearch : Silman_2008_Chem.Biol.Interact_175_3 |
| PubMedID: 18586019 |
Silman I, Sussman JL (2008)
Acetylcholinesterase: how is structure related to function?
Chemico-Biological Interactions
175 :3
Silman I, Sussman JL (2008)
Chemico-Biological Interactions
175 :3