L. Acetylcholinesterase: how is structure related to function?
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Acetylcholinesterase (AChE) is an enzyme that plays a crucial role in cholinergic transmission and synaptic function. It catalyzes the hydrolysis of the ester bond of acetylcholine. The structure of AChE is related to its function in several ways. The enzyme is a dimer, with each protomer consisting of two nonidentical chains . The active site of AChE is located in the α-chain, and the α and β chains together form an active unit . The active site contains an active-site serine residue at position 200 . The catalytically active groups are located at the bottom of a jaws-like slit with hydrophobic walls that provide substrate binding . AChE exists in multiple molecular forms, which differ in their quaternary structure and may be anchored to synaptic structures in different ways . These structural variations contribute to the specificity of AChE and its ability to perform its catalytic function .
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132 Citations | The paper discusses the atomic structure of acetylcholinesterase (AChE) and its catalytic mechanism, but it does not explicitly explain how the structure is related to its function. |
Open access 01 Dec 1986 18 Citations | The paper provides the amino acid sequence and structural information of acetylcholinesterase, but does not directly discuss the relationship between structure and function. |
15 Citations | The paper discusses the structure and function of acetylcholinesterase (ACh-ase). It mentions that ACh-ase is a dimer with two nonidentical chains and that the α-chain contains an active site. The function of ACh-ase is to hydrolyze acetylcholine (ACh) and allow the receptor to return to its original conformation, reestablishing the barrier of ion movements. |
| The paper discusses the influence of substrate leaving group structure on the effectiveness of acetylcholinesterase-catalyzed hydrolysis, but it does not directly address the relationship between the structure and function of acetylcholinesterase. |
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