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• W4323653612 abstract "Abstract Catalytic activity and function of acetylcholinesterase (AChE; EC 3.1.1.7) have been recognized and studied for over a century and its quaternary and primary structures for about half a century, and its tertiary structure has been known for about 33 years. Clear understanding of relationships between the structure and the function is still pending for this enzyme. Hundreds of crystallographic, static snapshots of AChEs from different sources reveal largely one general backbone conformation with narrow entry into the active center gorge, tightly fit to accept one acetylcholine (ACh) molecule, in contrast to its high catalytic turnover. This short review of available X‐ray structures of AChEs from electric ray Torpedo californica, mouse and human, finds some limited, yet consistent deviations in conformations of selected secondary structure elements of AChE relevant for its function. The observed conformational diversity of the acyl pocket loop of AChE, unlike the large Ω‐loop, appears consistent with structurally dynamic INS data and solution‐based SAXS experiments to explain its dominant role in controlling the size of the active center gorge opening, as well as connectivity between the immediate surroundings of the buried active Ser, and catalytically relevant sites on the AChE surface. image" @default.
• W4323653612 created "2023-03-10" @default.
• W4323653612 creator A5054200641 @default.
• W4323653612 date "2023-03-19" @default.
• W4323653612 modified "2023-10-17" @default.
• W4323653612 title "Connectivity between surface and interior in catalytic subunits of acetylcholinesterases inferred from their X‐ray structures" @default.
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• W4323653612 doi "https://doi.org/10.1111/jnc.15802" @default.
• W4323653612 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36892323" @default.
• W4323653612 hasPublicationYear "2023" @default.
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