Τίτλος:
Enzymatic removal of carboxyl protecting groups. 1. Cleavage of the tert-butyl moiety
Γλώσσες Τεκμηρίου:
Αγγλικά
Περίληψη:
(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.
Συγγραφείς:
Schmidt, M.
Barbayianni, E.
Fotakopoulou, I.
Höhne, M.
Constantinou-Kokotou, V.
Bornscheuer, U.T.
Kokotos, G.
Περιοδικό:
The Journal of Organic Chemistry
Λέξεις-κλειδιά:
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
