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• W1587638607 abstract "The apparent Km and Vmax of CMP-N-acetylneuraminate:lactosylceramide alpha 2,3-sialyltransferase (LacCer-alpha 2,3-ST) for lactosylceramide and CMP-N-acetylneuraminic acid were determined using 19 molecular species of lactosylceramide. The Km for lactosylceramide varied 6-fold among these molecular species of lactosylceramide, but there was a poor correlation between the Km for a particular molecular species and the activity of Lac-Cer alpha 2,3-ST for that molecular species. The Km for CMP-N-acetylneuraminic acid also varied depending on the molecular species of lactosylceramide used as substrate, and there was a good correlation between the Km of Lac-Cer alpha 2,3-ST for CMP-N-acetylneuraminic acid and the activity of the enzyme. Kinetic studies indicate that the reaction mechanism of LacCer alpha 2,3-ST is a sequential, Ordered Bi Bi system. From considerations of the effects of the structure of the lactosylceramide molecular species on the Vmax and Km for CMP-N-acetylneuraminic acid, it is likely that LacCer alpha 2,3-ST first binds lactosylceramide and then CMP-N-acetylneuraminic acid and that the rate-limiting step in the reaction is the release of the product GM3." @default.
• W1587638607 created "2016-06-24" @default.
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• W1587638607 date "1994-05-01" @default.
• W1587638607 modified "2023-09-29" @default.
• W1587638607 title "Mechanism of GM3 ganglioside synthesis. Kinetic study of rat liver CMP-N-neuraminate:lactosylceramide alpha 2,3-sialyltransferase employing 19 molecular species of lactosylceramide." @default.
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• W1587638607 doi "https://doi.org/10.1016/s0021-9258(17)36555-9" @default.
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