| Abstract
| - A recent discovery that a certain amino acid motif (GGG(A)X-motif) in lipases and esterases determines their activitytoward tertiary alcohols prompted us to investigate the useof these biocatalysts in the mild and selective removal oftert-butyl protecting groups in amino acid derivatives andrelated compounds. An esterase from Bacillus subtilis(BsubpNBE) and lipase A from Candida antarctica (CAL-A) were identified as the most active enzymes, whichhydrolyzed a range of tert-butyl esters of protected aminoacids (e.g., Boc-Tyr-OtBu, Z-GABA-OtBu, Fmoc-GABA-OtBu)in good to high yields and left Boc, Z, and Fmoc-protectinggroups intact.
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