TY - JOUR
TI - Enzymatic removal of carboxyl protecting groups. 1. Cleavage of the tert-butyl moiety
AU - Schmidt, M.
AU - Barbayianni, E.
AU - Fotakopoulou, I.
AU - Höhne, M.
AU - Constantinou-Kokotou, V.
AU - Bornscheuer, U.T.
AU - Kokotos, G.
JO - The Journal of Organic Chemistry
PY - 2005
VL - 70
TODO - 9
SP - 3737-3740
PB - 
SN - null
TODO - 10.1021/jo050114z
TODO - Alcohols;  Enzymes;  Esters;  Hydrolysis;  Reaction kinetics, Esterases;  Lipases;  Tert-butyl esters;  Tertiary alcohols, Amino acids, 9 fluorenylmethoxycarbonyl;  acid lipase;  amino acid derivative;  benzyloxycarbonyl;  carbonyl derivative;  esterase;  tert butyloxycarbonyl;  triacylglycerol lipase;  unclassified drug, article;  Bacillus subtilis;  biocatalyst;  Candida antarctica;  hydrolysis;  protein motif, Amino Acid Sequence;  Amino Acids;  Bacillus subtilis;  Benzene Derivatives;  Butanes;  Candida albicans;  Carboxylic Acids;  Catalysis;  Esterases;  Hydrocarbons, Halogenated;  Indicators and Reagents;  Lipase
TODO - (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.
ER -