Abstract
Amides of amino acids were hydrolyzed using hexose, pentose, and tetrose type glycolipids. They had a thiazolidine ring as the connecting group between a hydrophilic sugar moiety and a hydrophobic moiety (indirect type glycolipids) or did not have (direct type glycolipids). The former type glycolipid, in general, was more active than the latter type, and the activities, such as for substrate recognition and the hydrolyzing activity, were found to relate to the configuration of hydroxyl groups on C-2 and C-3 positions of the sugar moiety. That is, the L-threo type glycolipids showed the highest activities in both characteristics, and the D-threo type showed the lowest activities. The erythro type glycolipids exhibited moderate activities.
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