Enzymatic removal of carboxyl protecting groups. 1. Cleavage of the tert-butyl moiety

• Main Authors: Schmidt, M., Barbayianni, E., Fotakopoulou, I., Höhne, M., Constantinou-Kokotou, V., Bornscheuer, U.T., Kokotos, G.
• Format: Article in Journal/Newspaper
• Language: English
• Published: 2005
• Subjects: Antarc*; Antarctica
• Online Access: https://pergamos.lib.uoa.gr/uoa/dl/object/uoadl:3067967

(Chemical Equation Presented) A recent discovery that a certain amino acid motif (GGG-(A)X-motif) in lipases and esterases determines their activity toward tertiary alcohols prompted us to investigate the use of these biocatalysts in the mild and selective removal of tert-butyl protecting groups in amino acid derivatives and related compounds. An esterase from Bacillus subtilis (BsubpNBE) and lipase A from Candida antarctica (CAL-A) were identified as the most active enzymes, which hydrolyzed a range of tert-butyl esters of protected amino acids (e.g., Boc-Tyr-OtBu, Z-GABA-OtBu, Fmoc-GABA-O tBu) in good to high yields and left Boc, Z, and Fmoc-protecting groups intact. © 2005 American Chemical Society.