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- W2021322379 abstract "Abstract The solid-state structures of the zwitterionic forms of both carnitine and acetylcarnitine have been determined by single-crystal X-ray analysis. The crystal structure of acetylcarnitine reveals a different backbone conformation from that of carnitine. The conformational differences observed for carnitine and acetylcarnitine are more a consequence of steric than electrostatic effects. A detailed comparison is made between the zwietterionic structures and previously published hydrochloride salts. The effect of charge distribution on conformation is discussed. The zwitterionic structures do not exhibit enhanced electrostatic attraction between carboxylate and quaternary ammonium portions of the molecules. Finally, a hypothesis is presented for the mode of binding of carnitine (or acetylcarnitine) to the enzyme, carnitine acetyltransferase. Based on this model for binding, a speculative topographic description of the enzymatic mechanism is presented." @default.
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- W2021322379 date "1985-09-01" @default.
- W2021322379 modified "2023-09-27" @default.
- W2021322379 title "Crystal structures of carnitine and acetylcarnitine zwitterions: A structural hypothesis for mode of action" @default.
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- W2021322379 doi "https://doi.org/10.1016/0045-2068(85)90022-7" @default.
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