Add time:07/18/2019         Source:sciencedirect.com

Dithiothreitol was found to be a competitive inhibitor for a purified L-fucose isomerase from Aerobacteraerogenes, inhibiting enzyme activity for the isomerization of both L-fucose and D-arabinose. The kinetics of inhibition showed that the oxidized form was the more potent inhibitor. The Ki for both sugars was the same. Dithioerythitol and certain polyalcoholic sugars also appeared to function as competitive inhibitors of the enzyme.

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