Abstract
AbstractQuinic acid (1a), shikimic acid (2), and their derivatives were acylated in organic solvents by several lipases and by the protease subtilisin Carlsberg. The most satisfactory results were obtained with methyl (or benzyl) quinate (7a (or 8a)) and lipase from Chromobacterium viscosum adsorbed on Celite, which showed an overshelming preference towards the acylation of OH–C(4). Under optimized conditions, the syntehtically useful 4‐O ‐acetylquinate 8d was isolated in ca. 90% yield. On the other hand, acylation of methyl shikimate (10a) showed no regioselectivity with any of the enzymes tested. A possible rationale for the different behavior of Chromobacterium viscosum lipase towards 7a and 10a is given, comparing the conformations of these two molecules, as deducted from 1H‐NMR and molecular‐mechanics calculation.
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