@article{3067967,
    title = "Enzymatic removal of carboxyl protecting groups. 1. Cleavage of the tert-butyl moiety",
    author = "Schmidt, M. and Barbayianni, E. and Fotakopoulou, I. and Höhne, M. and Constantinou-Kokotou, V. and Bornscheuer, U.T. and Kokotos, G.",
    journal = "The Journal of Organic Chemistry",
    year = "2005",
    volume = "70",
    number = "9",
    pages = "3737-3740",
    doi = "10.1021/jo050114z",
    keywords = "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",
    abstract = "(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."
}